# enzymes

entry: 2.7.11.3
sysname: ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase
iubmb_reaction: R04589
name:
--- 
- dephospho-[reductase kinase] kinase
- AMP-activated kinase
- AMP-activated protein kinase kinase
- hydroxymethylglutaryl coenzyme A reductase kinase kinase
- hydroxymethylglutaryl coenzyme A reductase kinase kinase (phosphorylating)
- reductase kinase
- reductase kinase kinase
- STK30

comment:
The enzyme is activated by AMP and is specific for its substrate. Phosphorylates and activates EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, that has been inactivated by EC 3.1.3.16, phosphoprotein phosphatase.

reaction:
ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} = ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} [RN:R04589]


entry: 2.7.11.4
sysname: ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphotransferase
iubmb_reaction: (other) R03516
kegg_reaction: R03516
name:
--- 
- "[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase"
- BCK
- BCKD kinase
- BCODH kinase
- branched-chain alpha-ketoacid dehydrogenase kinase
- branched-chain 2-oxo acid dehydrogenase kinase
- branched-chain keto acid dehydrogenase kinase
- branched-chain oxo acid dehydrogenase kinase (phosphorylating)
- STK2

comment:
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation inactivates EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).

reaction:
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate


entry: 2.7.11.5
sysname: ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase
iubmb_reaction: R04401
name:
--- 
- "[isocitrate dehydrogenase (NADP+)] kinase"
- "[isocitrate dehydrogenase (NADP)] kinase"
- ICDH kinase/phosphatase
- IDH kinase
- IDH kinase/phosphatase
- IDH-K/P
- IDHK/P
- isocitrate dehydrogenase kinase (phosphorylating)
- isocitrate dehydrogenase kinase/phosphatase
- STK3

comment:
The enzyme has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate dehydrogenase (NADP+).

reaction:
ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate [RN:R04401]


entry: 2.7.11.6
sysname: ATP:[tyrosine-3-monoxygenase] phosphotransferase
reaction: ATP + [tyrosine-3-monooxygenase] = ADP + phospho-[tyrosine-3-monooxygenase]
iubmb_reaction: (other) R04275
kegg_reaction: R04275
name:
--- 
- "[tyrosine 3-monooxygenase] kinase"
- pheochromocytoma tyrosine hydroxylase-associated kinase
- STK4
- tyrosine 3-monooxygenase kinase (phosphorylating)

comment:
The enzyme has no activating compound but is specific for its substrate, with which it co-purifies. Requires Mg2+. Activates EC 1.14.16.2, tyrosine 3-monooxygenase, by phosphorylation.


entry: 2.7.11.7
sysname: ATP:[myosin heavy-chain] O-phosphotransferase
reaction: ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
iubmb_reaction: (other) R04023
kegg_reaction: R04023
name:
--- 
- myosin-heavy-chain kinase
- ATP:myosin-heavy-chain O-phosphotransferase
- calmodulin-dependent myosin heavy chain kinase
- MHCK
- MIHC kinase
- myosin heavy chain kinase
- myosin I heavy-chain kinase
- myosin II heavy-chain kinase
- "[myosin-heavy-chain] kinase"
- myosin heavy chain kinase A
- STK6

comment:
The enzyme from Dictyostelium sp. (slime moulds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin. One threonine residue in each heavy chain acts as acceptor. While the enzyme from some species is activated by actin, in other cases Ca2+/calmodulin are required for activity.


entry: 2.7.11.8
name: --- - Fas-activated serine/threonine kinase - FAST - FASTK - STK10
sysname: ATP:[Fas-activated serine/threonine protein] phosphotransferase
iubmb_reaction: (other) R00162
kegg_reaction: R00162
comment:
This enzyme is activated during Fas-mediated apoptosis. Following Fas ligation, the enzyme, which is constitutively phosphorylated, is dephosphorylated, and it is the dephosphorylated form that causes phosphorylation of TIA-1, a nuclear RNA-binding protein. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation.

reaction:
ATP + [Fas-activated serine/threonine protein] = ADP + [Fas-activated serine/threonine phosphoprotein]


entry: 2.7.11.9
sysname: ATP:[Goodpasture antigen-binding protein] phosphotransferase
reaction: ATP + [Goodpasture antigen-binding protein] = ADP + [Goodpasture antigen-binding phosphoprotein]
iubmb_reaction: (other) R00162
kegg_reaction: R00162
name:
--- 
- Goodpasture-antigen-binding protein kinase
- GPBPK
- GPBP kinase
- STK11
- Goodpasture antigen-binding protein kinase

comment:
This serine/threonine kinase specifically binds to and phosphorylates the N-terminal region of the human Goodpasture antigen, which is located on the alpha3 chain of collagen IV and is involved in autoimmune disease.


entry: 2.7.11.10
sysname: ATP:[IkappaB protein] phosphotransferase
reaction: ATP + [IkappaB protein] = ADP + [IkappaB phosphoprotein]
iubmb_reaction: (other) R00162
kegg_reaction: R00162
name:
--- 
- IkappaB kinase
- CHUK
- IKBKA
- IKBKB
- IKK
- IKK-1
- IKK-2
- inhibitor of NFkappaB kinase
- inhibitor of NF-kappaB kinase
- STK12
- TANK-binding kinase 1
- TBK1

comment:
The enzyme phosphorylates IkappaB proteins at specific serine residues, which marks them for destruction via the ubiquitination pathway. Subsequent degradation of the IkB complex (IKK) activates NF-kappaB, a translation factor that plays an important role in inflammation, immunity, cell proliferation and apoptosis. If the serine residues are replaced by threonine residues, the activity of the enzyme is decreased considerably.


entry: 2.7.11.11
name: --- - cAMP-dependent protein kinase - AMPK - PKA - PKA C - protein kinase A - STK22
sysname: ATP:protein phosphotransferase (cAMP-dependent)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
comment:
cAMP is required to activate this enzyme. The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits [i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C].


entry: 2.7.11.12
sysname: ATP:protein phosphotransferase (cGMP-dependent)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- cGMP-dependent protein kinase
- 3':5'-cyclic GMP-dependent protein kinase
- cGMP-dependent protein kinase Ibeta
- guanosine 3':5'-cyclic monophosphate-dependent protein kinase
- PKG
- PKG 1alpha
- PKG 1beta
- PKG II
- STK23

comment:
cGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].


entry: 2.7.11.13
sysname: ATP:protein phosphotransferase (diacylglycerol-dependent)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- protein kinase C
- calcium-dependent protein kinase C
- calcium-independent protein kinase C
- calcium/phospholipid dependent protein kinase
- cPKCalpha
- cPKCbeta
- cPKCgamma
- nPKCdelta
- nPKCepsilon
- nPKCh
- nPKCtheta
- PKC
- PKCalpha
- PKCbeta
- PKCgamma
- PKCdelta
- PKCepsilon
- PKCzeta
- Pkc1p
- protein kinase Cepsilon
- STK24

comment:
A family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signalling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumour promoters.


entry: 2.7.11.14
sysname: ATP:rhodopsin phosphotransferase
reaction: ATP + rhodopsin = ADP + phosphorhodopsin [RN:R02903]
iubmb_reaction: R02903
name:
--- 
- rhodopsin kinase
- cone opsin kinase
- G-protein-coupled receptor kinase 1
- GPCR kinase 1
- GRK1
- GRK7
- opsin kinase
- opsin kinase (phosphorylating)
- rhodopsin kinase (phosphorylating)
- RK
- STK14

comment:
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the bleached or activated form of rhodopsin; also phosphorylates the beta-adrenergic receptor, but more slowly. Does not act on casein, histones or phosphvitin. Inhibited by Zn2+ and digitonin (cf. EC 2.7.11.15, beta-adrenergic-receptor kinase and EC 2.7.11.16, G-protein-coupled receptor kinase).


entry: 2.7.11.15
sysname: ATP:[beta-adrenergic receptor] phosphotransferase
reaction: ATP + [beta-adrenergic receptor] = ADP + phospho-[beta-adrenergic receptor] [RN:R03274]
iubmb_reaction: R03274
name:
--- 
- beta-adrenergic-receptor kinase
- ATP:beta-adrenergic-receptor phosphotransferase
- "[beta-adrenergic-receptor] kinase"
- beta-adrenergic receptor-specific kinase
- beta-AR kinase
- beta-ARK
- beta-ARK 1
- beta-ARK 2
- beta-receptor kinase
- GRK2
- GRK3
- beta-adrenergic-receptor kinase (phosphorylating)
- beta2ARK
- betaARK1
- beta-adrenoceptor kinase
- beta-adrenoceptor kinase 1
- beta-adrenoceptor kinase 2
- ADRBK1
- BARK1
- adrenergic receptor kinase
- STK15

comment:
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly. Does not act on casein or histones. The enzyme is inhibited by Zn2+ and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14, rhodopsin kinase and EC 2.7.11.16, G-protein-coupled receptor kinase).


entry: 2.7.11.16
sysname: ATP:[G-protein-coupled receptor] phosphotransferase
reaction: ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate
name:
--- 
- G-protein-coupled receptor kinase
- G protein-coupled receptor kinase
- GPCR kinase
- GPCRK
- GRK4
- GRK5
- GRK6
- STK16

comment:
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). All members of this enzyme subfamily possess a highly conserved binding site for 1-phosphatidylinositol 4,5-bisphosphate. (cf. EC 2.7.11.14, rhodopsin kinase and EC 2.7.11.15, beta-adrenergic-receptor kinase).


entry: 2.7.11.17
sysname: ATP:protein phosphotransferase (Ca2+/calmodulin-dependent)
reaction: ATP + a protein = ADP + a phosphoprotein
iubmb_reaction: (other) R00162
kegg_reaction: R00162
name:
--- 
- Ca2+/calmodulin-dependent protein kinase
- ATP:caldesmon O-phosphotransferase
- caldesmon kinase
- caldesmon kinase (phosphorylating)
- Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase
- Ca2+/calmodulin-dependent protein kinase 1
- Ca2+/calmodulin-dependent protein kinase II
- Ca2+/calmodulin-dependent protein kinase IV
- Ca2+/calmodulin-dependent protein kinase kinase
- Ca2+/calmodulin-dependent protein kinase kinase beta
- calmodulin-dependent kinase II
- CaM kinase
- CaM kinase II
- CAM PKII
- CaM-regulated serine/threonine kinase
- CaMKI
- CaMKII
- CaMKIV
- CaMKKalpha
- CaMKKbeta
- microtubule-associated protein 2 kinase
- STK20

comment:
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase).


entry: 2.7.11.18
sysname: ATP:[myosin light chain] O-phosphotransferase
reaction: ATP + [myosin light chain] = ADP + [myosin light chain] phosphate [RN:R03150]
iubmb_reaction: R03150
name:
--- 
- myosin-light-chain kinase
- "[myosin-light-chain] kinase"
- ATP:myosin-light-chain O-phosphotransferase
- calcium/calmodulin-dependent myosin light chain kinase
- MLCK
- MLCKase
- myosin kinase
- myosin light chain kinase
- myosin light chain protein kinase
- myosin light-chain kinase (phosphorylating)
- smooth-muscle-myosin-light-chain kinase
- STK18

comment:
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.


entry: 2.7.11.19
sysname: ATP:phosphorylase-b phosphotransferase
reaction: 2 ATP + phosphorylase b = 2 ADP + phosphorylase a [RN:R00076]
iubmb_reaction: R00076
name:
--- 
- phosphorylase kinase
- dephosphophosphorylase kinase
- glycogen phosphorylase kinase
- PHK
- phosphorylase b kinase
- phosphorylase B kinase
- phosphorylase kinase (phosphorylating)
- STK17

comment:
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis-glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The gamma subunit of the tetrameric alpha,beta,gamma,delta enzyme is the catalytic subunit.


entry: 2.7.11.20
sysname: ATP:[elongation factor 2] phosphotransferase
reaction: ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate
name:
--- 
- elongation factor 2 kinase
- Ca/CaM-kinase III
- calmodulin-dependent protein kinase III
- CaM kinase III
- eEF2 kinase
- eEF2K
- EF2K
- STK19

comment:
Requires Ca2+ and calmodulin for activity. The enzyme can also be phosphorylated by the catalytic subunit of EC 2.7.11.11, cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca2+ [1,2].


entry: 2.7.11.21
sysname: ATP:protein phosphotransferase (spindle-pole-dependent)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- polo kinase
- Cdc5
- Cdc5p
- Plk
- PLK
- Plk1
- Plo1
- POLO kinase
- polo serine-threonine kinase
- polo-like kinase
- polo-like kinase 1
- serine/threonine-specific Drosophila kinase polo
- STK21

comment:
The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein [2].


entry: 2.7.11.22
sysname: ATP:cyclin phosphotransferase
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- cyclin-dependent kinase
- Bur1
- Bur1 Cdk
- Cak1
- Cak1p
- cdc2
- cdc2 kinase
- Cdc28p
- CDK
- cdk-activating kinase
- Cdk-activating protein kinase
- cdk1
- cdk2
- Cdk2
- cdk3
- cdk4
- cdk5
- cdk6
- cdk7
- cdk8
- cdk9
- cyclin A-activated cdc2
- cyclin A-activated cdk2
- cyclin D-cdk6 kinase
- cyclin D-dependent kinase
- cyclin E kinase
- cyclin-A associated kinase
- cyclin-dependent kinase 6
- cyclin-dependent kinase-2
- cyclin-dependent kinase-4
- cyclin-dependent protein kinase activating kinase
- cyk
- D-type cyclin kinase
- nclk
- neuronal cdc2-like kinase
- PCTAIRE-1
- STK25

comment:
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.


entry: 2.7.11.23
name: --- - "[RNA-polymerase]-subunit kinase" - CTD kinase - STK9
sysname: ATP:[DNA-directed RNA polymerase] phosphotransferase
reaction: ATP + [DNA-directed RNA polymerase] = ADP + phospho-[DNA-directed RNA polymerase] [RN:R04358]
iubmb_reaction: R04358
comment:
The enzyme appears to be distinct from other protein kinases. It brings about multiple phosphorylations of the unique C-terminal repeat domain of the largest subunit of eukaryotic DNA-directed RNA polymerase (EC 2.7.7.6). The enzyme does not phosphorylate casein, phosvitin or histone.


entry: 2.7.11.24
sysname: ATP:protein phosphotransferase (MAPKK-activated)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- mitogen-activated protein kinase
- c-Jun N-terminal kinase
- Dp38
- ERK
- ERK1
- ERK2
- extracellular signal-regulated kinase
- JNK
- JNK3alpha1
- LeMPK3
- MAP kinase
- MAP-2 kinase
- MAPK
- MBP kinase I
- MBP kinase II
- microtubule-associated protein 2 kinase
- microtubule-associated protein kinase
- myelin basic protein kinase
- p38delta
- p38-2
- p42 mitogen-activated protein kinase
- p42mapk
- PMK-1
- PMK-2
- PMK-3
- pp42
- pp44mapk
- p44mpk
- SAPK
- STK26
- stress-activated protein kinase

comment:
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.


entry: 2.7.11.25
sysname: ATP:protein phosphotransferase (MAPKKKK-activated)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- mitogen-activated protein kinase kinase kinase
- cMos
- cRaf
- MAPKKK
- MAP3K
- MAP kinase kinase kinase
- MEKK
- MEKK1
- MEKK2
- MEKK3
- MEK kinase
- Mil/Raf
- MLK-like mitogen-activated protein triple kinase
- MLTK
- MLTKa
- MLTKb
- REKS
- STK28

comment:
This enzyme phosphorylates and activates its downstream protein kinase, EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) but requires MAPKKKK for activation. Some members of this family can be activated by p21-activated kinases (PAK/STE20) or Ras. While c-Raf and c-Mos activate the classical MAPK/ERK pathway, MEKK1 and MEKK2 preferentially activate the c-Jun N-terminal protein kinase(JNK)/stress-activated protein kinase (SAPK) pathway [2]. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.


entry: 2.7.11.26
sysname: ATP:[tau-protein] O-phosphotransferase
reaction: ATP + [tau-protein] = ADP + O-phospho-[tau-protein]
iubmb_reaction: (other) R03744
kegg_reaction: R03744
name:
--- 
- tau-protein kinase
- ATP:tau-protein O-hosphotransferase
- brain protein kinase PK40erk
- cdk5/p20
- CDK5/p23
- glycogen synthase kinase-3beta
- GSK
- protein tau kinase
- STK31
- tau kinase
- "[tau-protein] kinase"
- tau-protein kinase I
- tau-protein kinase II
- tau-tubulin kinase
- TPK
- TPK I
- TPK II
- TTK

comment:
Activated by tubulin. Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.


entry: 2.7.11.27
sysname: ATP:[acetyl-CoA carboxylase] phosphotransferase
reaction: ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate [RN:R03272]
iubmb_reaction: R03272
name:
--- 
- "[acetyl-CoA carboxylase] kinase"
- acetyl coenzyme A carboxylase kinase (phosphorylating)
- acetyl-CoA carboxylase bound kinase
- acetyl-CoA carboxylase kinase
- acetyl-CoA carboxylase kinase (cAMP-independent)
- acetyl-CoA carboxylase kinase 2
- acetyl-CoA carboxylase kinase-2
- acetyl-CoA carboxylase kinase-3 (AMP-activated)
- acetyl-coenzyme A carboxylase kinase
- ACK2
- ACK3
- AMPK
- I-peptide kinase
- STK5

comment:
Phosphorylates and inactivates EC 6.4.1.2, acetyl-CoA carboxylase, which can be dephosphorylated and reactivated by EC 3.1.3.17, [phosphorylase] phosphatase. The enzyme is more active towards the dimeric form of acetyl-CoA carboxylase than the polymeric form [5]. Phosphorylates serine residues.


entry: 2.7.11.28
name: --- - tropomyosin kinase - tropomyosin kinase (phosphorylating) - STK
sysname: ATP:tropomyosin O-phosphotransferase
reaction: ATP + tropomyosin = ADP + O-phosphotropomyosin [RN:R02980]
iubmb_reaction: R02980
comment:
The enzyme phosphorylates casein equally well, and histone and phosvitin to a lesser extent. The acceptor is a serine residue in the protein.


entry: 2.7.11.29
sysname: ATP:[low-density-lipoprotein receptor]-L-serine O-phosphotransferase
iubmb_reaction: (other) R04403
kegg_reaction: R04403
name:
--- 
- low-density-lipoprotein-receptor kinase
- ATP:low-density-lipoprotein-L-serine O-phosphotransferase
- LDL receptor kinase
- "[low-density-lipoprotein] kinase"
- low-density lipoprotein kinase
- low-density-lipoprotein receptor kinase (phosphorylating)
- STK7

comment:
Phosphorylates the last serine residue (Ser-833) in the cytoplasmic domain of the low-density lipoprotein receptor from bovine adrenal cortex. Casein can also act as a substrate but with lower affinity. GTP can act instead of ATP.

reaction:
ATP + [low-density-lipoprotein receptor]-L-serine = ADP + [low-density-lipoprotein receptor]-O-phospho-L-serine


entry: 2.7.11.30
sysname: ATP:[receptor-protein] phosphotransferase
reaction: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
iubmb_reaction: (other) R00162
kegg_reaction: R00162
name:
--- 
- receptor protein serine/threonine kinase
- activin receptor kinase
- receptor type I serine/threonine protein kinase
- receptor type II serine/threonine protein kinase
- STK13
- TGF-beta kinase
- receptor serine/threonine protein kinase

comment:
The transforming growth factor beta (TGF-beta) family of cytokines regulates cell proliferation, differentiation, recognition and death. Signalling occurs by the binding of ligand to the type II receptor, which is the constitutively active kinase. Bound TGF-beta is then recognized by receptor I, which is phosphorylated and can propagate the signal to downstream substrates [1,3].


entry: 2.7.11.31
sysname: ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
iubmb_reaction: R04555
name:
--- 
- "[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase"
- AMPK
- AMP-activated protein kinase
- HMG-CoA reductase kinase
- beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
- "[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase"
- 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
- 3-hydroxy-3-methylglutaryl-CoA reductase kinase
- hydroxymethylglutaryl coenzyme A reductase kinase
- hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
- hydroxymethylglutaryl-CoA reductase kinase
- reductase kinase
- STK29

comment:
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase [7]. GTP can act instead of ATP [4]

reaction:
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate [RN:R04555]


entry: 2.7.12.1
sysname: ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
comment: This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- dual-specificity kinase
- ADK1
- Arabidopsis dual specificity kinase 1
- CLK1
- dDYRK2
- Mps1p


entry: 2.7.12.2
sysname: ATP:protein phosphotransferase (MAPKKK-activated)
reaction: ATP + a protein = ADP + a phosphoprotein [RN:R00162]
iubmb_reaction: R00162
name:
--- 
- mitogen-activated protein kinase kinase
- MAP kinase kinase
- MAP kinase kinase 4
- MAP kinase kinase 7
- MAP kinase or ERK kinase
- MAP2K
- MAPKK
- MAPKK1
- MEK
- MEK1
- MEK2
- MKK
- MKK2
- MKK4
- MKK6
- MKK7
- STK27

comment:
This enzyme is a dual-specific protein kinase and requires mitogen-activated protein kinase kinase kinase (MAPKKK) for activation. It is required for activation of EC 2.7.11.24, mitogen-activated protein kinase. Phosphorylation of MEK1 by Raf involves phosphorylation of two serine residues [5]. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.


entry: 2.7.13.1
sysname: ATP:protein-L-histidine N(pi)-phosphotransferase
comment: A number of histones can act as acceptor.
reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine [RN:R02625]
iubmb_reaction: R02625
name:
--- 
- protein-histidine pros-kinase
- ATP:protein-L-histidine N-pros-phosphotransferase
- histidine kinase (ambiguous)
- histidine protein kinase (ambiguous)
- protein histidine kinase (ambiguous)
- protein kinase (histidine) (ambiguous)
- HK2


entry: 2.7.13.2
sysname: ATP:protein-L-histidine N(tau)-phosphotransferase
comment: A number of histones can act as acceptor.
reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine [RN:R02626]
iubmb_reaction: R02626
name:
--- 
- protein-histidine tele-kinase
- ATP:protein-L-histidine N-tele-phosphotransferase
- histidine kinase (ambiguous)
- histidine protein kinase (ambiguous)
- protein histidine kinase (ambiguous)
- protein kinase (histidine) (ambiguous)
- HK3


entry: 2.7.13.3
sysname: ATP:protein-L-histidine N-phosphotransferase
reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
name:
--- 
- histidine kinase
- EnvZ
- histidine kinase (ambiguous)
- histidine protein kinase (ambiguous)
- protein histidine kinase (ambiguous)
- protein kinase (histidine) (ambiguous)
- HK1
- HP165
- Sln1p

comment:
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.


entry: 2.7.99.1
sysname: triphosphate:[microsomal-membrane-protein] phosphotransferase
iubmb_reaction: R04312
name:
--- 
- triphosphate-protein phosphotransferase
- diphosphate:microsomal-membrane-protein O-phosphotransferase (erroneous)
- DiPPT (erroneous)
- pyrophosphate:protein phosphotransferase (erroneous)
- diphosphate-protein phosphotransferase (erroneous)
- diphosphate:[microsomal-membrane-protein] O-phosphotransferase (erroneous)

comment:
This enzyme was originally thought to use diphosphate as substrate [1] but this has since been disproved [2]. The activity is observed as the second part of a biphasic reaction after depletion of ATP. Tripolyphosphate is a contaminant of [gamma-32P]ATP.

reaction:
triphosphate + [microsomal-membrane protein] = diphosphate + phospho-[microsomal-membrane protein] [RN:R04312]


entry: 2.7.-.-
name: --- []
reaction:
(1) ATP + D-glycero-D-manno-Heptose 1-phosphate <=> Pyrophosphate + ADP-D-glycero-D-manno-heptose [RN:R05644]; (2) ATP + D-glycero-D-manno-Heptose 7-phosphate <=> ADP + D-glycero-D-manno-Heptose 1,7-bisphosphate [RN:R05646]; (3) Phosphatidylethanolamine + G00141 <=> Diacylglycerol + G00151 [RN:R05924]


entry: 2.8.1.1
sysname: thiosulfate:cyanide sulfurtransferase
comment: A few other sulfur compounds can act as donors.
reaction: thiosulfate + cyanide = sulfite + thiocyanate [RN:R01931]
iubmb_reaction: R01931
name:
--- 
- thiosulfate sulfurtransferase
- thiosulfate cyanide transsulfurase
- thiosulfate thiotransferase
- rhodanese
- rhodanase


entry: 2.8.1.2
name: --- - 3-mercaptopyruvate sulfurtransferase - beta-mercaptopyruvate sulfurtransferase
sysname: 3-mercaptopyruvate:cyanide sulfurtransferase
reaction: 3-mercaptopyruvate + cyanide = pyruvate + thiocyanate [RN:R07286]
iubmb_reaction: R07286
kegg_reaction: R03105 R05208
comment:
Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. The bacterial enzyme is a zinc protein.


entry: 2.8.1.3
sysname: thiosulfate:thiol sulfurtransferase
reaction: thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide [RN:R01875]
iubmb_reaction: R01875
name:
--- 
- thiosulfate-thiol sulfurtransferase
- glutathione-dependent thiosulfate reductase
- sulfane reductase
- sulfane sulfurtransferase

comment:
The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. L-Cysteine can also act as acceptor.


entry: 2.8.1.4
sysname: L-cysteine:tRNA sulfurtransferase
reaction: L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide [RN:R03923]
iubmb_reaction: R03923
name:
--- 
- tRNA sulfurtransferase
- transfer ribonucleate sulfurtransferase
- RNA sulfurtransferase
- ribonucleate sulfurtransferase
- transfer RNA sulfurtransferase
- transfer RNA thiolase

comment:
A group of enzymes transferring sulfur to various nucleotides in a tRNA chain, producing residues such as 4-thiouridylate. With some enzymes mercaptopyruvate can act as sulfur donor.


entry: 2.8.1.5
name: --- - thiosulfate-dithiol sulfurtransferase - thiosulfate reductase - TSR
sysname: thiosulfate:dithioerythritol sulfurtransferase
iubmb_reaction: (other) R03085 R05072
kegg_reaction: R03085 R05072
comment:
The enzyme from Chlorella shows very little activity towards monothiols such as glutathione and cysteine (cf. EC 2.8.1.3 thiosulfate-thiolsulfurtransferase). The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S-, and sulfide is spontaneously expelled from this by reaction with the other thiol group. May be identical with EC 2.8.1.1 thiosulfate sulfurtransferase.

reaction:
thiosulfate + dithioerythritol = sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized dithioerythritol) + sulfide


entry: 2.8.1.6
name: --- - biotin synthase
sysname: dethiobiotin:sulfur sulfurtransferase
iubmb_reaction: R01078
comment:
This single-turnover enzyme is a member of the 'radical SAM' (S-adenosylmethionine; AdoMet) family, all members of which contain the motif CX3CX2C. The enzyme contains a [2Fe-2S] and a [4Fe-4S] centre. The [4Fe-4S]2+,+ complex mediates the electron transfer required for the reductive cleavage of AdoMet into methionine and a deoxyadenosyl radical. Two molecules of AdoMet are consumed to activate positions 6 and 9 of dethiobiotin. This is required to abstract a hydrogen atom, which is then replaced by the sulfur atom at postition C-6. Sulfur insertion into dethiobiotin takes place with retention of configuration [3]. The sulfur donor has not been identified to date - it is neither elemental sulfur nor from SAM, but it has been postulated that it may be from the [2Fe-2S] centre [4].

reaction:
dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosyl radicals [RN:R01078]


entry: 2.8.1.7
name: --- - cysteine desulfurase - IscS - NIFS - NifS - SufS - cysteine desulfurylase
sysname: L-cysteine:[enzyme cysteine] sulfurtransferase
reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
iubmb_reaction: (other) R07460
kegg_reaction: R07460
comment:
A pyridoxal-phosphate protein. The reaction shown is the first part of a catalytic reaction, which is completed by passing on its extra sulfur to other acceptors. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1]. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur [2].


entry: 2.8.1.8
name: --- - lipoyl synthase - LS - LipA
sysname: protein N6-(octanoyl)lysine:sulfur sulfurtransferase
comment:
This enzyme is a member of the 'radical SAM' (S-adenosylmethionine; AdoMet) family, all members of which contain the motif CX3CX2C. Catalyses the final step in the de-novo biosynthesis of the lipoyl cofactor, which is the insertion of two sulfur atoms into an eight-carbon saturated fatty-acyl chain at C-6 and C-8. The lipoyl cofactor is essential for the function of several key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,5]. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and a 5'-deoxyadenosyl radical. The high-energy 5'-deoxyadenosyl radical then initiates catalysis by abstracting a key hydrogen atom from the relevant substrate [1]. The sulfur atoms are inserted with inversion of configuration [4]. The other enzymes involved in the biosynthesis of lipoyl cofactor are EC 2.3.1.181, lipoyl(octanoyl) transferase and EC 2.7.7.63, lipoate-protein ligase.

reaction:
protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl radicals


entry: 2.8.2.1
sysname: 3'-phosphoadenylyl-sulfate:phenol sulfotransferase
reaction: 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
iubmb_reaction: (other) R01242
kegg_reaction: R01242
name:
--- 
- aryl sulfotransferase
- phenol sulfotransferase
- sulfokinase
- 1-naphthol phenol sulfotransferase
- 2-naphtholsulfotransferase
- 4-nitrocatechol sulfokinase
- arylsulfotransferase
- dopamine sulfotransferase
- p-nitrophenol sulfotransferase
- phenol sulfokinase
- ritodrine sulfotransferase
- PST

comment:
A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).


entry: 2.8.2.2
sysname: 3'-phosphoadenylyl-sulfate:alcohol sulfotransferase
iubmb_reaction: R00629
kegg_reaction: R03405
name:
--- 
- alcohol sulfotransferase
- hydroxysteroid sulfotransferase
- 3beta-hydroxy steroid sulfotransferase
- delta5-3beta-hydroxysteroid sulfokinase
- 3-hydroxysteroid sulfotransferase
- HST
- 5alpha-androstenol sulfotransferase
- cholesterol sulfotransferase
- dehydroepiandrosterone sulfotransferase
- estrogen sulfokinase
- estrogen sulfotransferase
- steroid alcohol sulfotransferase
- steroid sulfokinase
- steroid sulfotransferase
- sterol sulfokinase
- sterol sulfotransferase
- alcohol/hydroxysteroid sulfotransferase
- 3beta-hydroxysteroid sulfotransferase

comment:
Primary and secondary alcohols, including aliphatic alcohols, ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid sulfotransferase).

reaction:
3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate [RN:R00629]


entry: 2.8.2.3
name: --- - amine sulfotransferase - arylamine sulfotransferase - amine N-sulfotransferase
sysname: 3'-phosphoadenylyl-sulfate:amine N-sulfotransferase
reaction: 3'-phosphoadenylyl sulfate + an amine = adenosine 3',5'-bisphosphate + a sulfamate [RN:R02809]
iubmb_reaction: R02809 > R01861
comment:
A large number of primary and secondary amines can act as acceptors, including aniline, 2-naphthylamine, cyclohexylamine and octylamine.


entry: 2.8.2.4
sysname: 3'-phosphoadenylyl-sulfate:estrone 3-sulfotransferase
reaction: 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate [RN:R02350]
iubmb_reaction: R02350
name:
--- 
- estrone sulfotransferase
- 3'-phosphoadenylyl sulfate-estrone 3-sulfotransferase
- estrogen sulfotransferase
- estrogen sulphotransferase
- oestrogen sulphotransferase
- 3'-phosphoadenylylsulfate:oestrone sulfotransferase


entry: 2.8.2.5
name: --- - chondroitin 4-sulfotransferase - chondroitin sulfotransferase
sysname: 3'-phosphoadenylyl-sulfate:chondroitin 4'-sulfotransferase
iubmb_reaction: R02180
comment:
The sulfation takes place at the 4-position of N-acetyl-galactosamine residues of chondroitin. Not identical with EC 2.8.2.17 chondroitin 6-sulfotransferase.

reaction:
3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]


entry: 2.8.2.7
sysname: 3'-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate 6-sulfotransferase
iubmb_reaction: R04476
name:
--- 
- UDP-N-acetylgalactosamine-4-sulfate sulfotransferase
- uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase
- uridine diphospho-N-acetylgalactosamine 4-sulfate sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + UDP-N-acetyl-D-galactosamine 4-sulfate = adenosine 3',5'-bisphosphate + UDP-N-acetyl-D-galactosamine 4,6-bissulfate [RN:R04476]


entry: 2.8.2.8
sysname: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfotransferase
iubmb_reaction: (other) R02122
kegg_reaction: R02122
name:
--- 
- "[heparan sulfate]-glucosamine N-sulfotransferase"
- heparin N-sulfotransferase
- 3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase
- PAPS:N-desulfoheparin sulfotransferase
- PAPS:DSH sulfotransferase
- N-HSST
- N-heparan sulfate sulfotransferase
- heparan sulfate N-deacetylase/N-sulfotransferase
- heparan sulfate 2-N-sulfotransferase
- heparan sulfate N-sulfotransferase
- heparan sulfate sulfotransferase
- N-desulfoheparin sulfotransferase
- desulfoheparin sulfotransferase
- 3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase
- heparitin sulfotransferase
- 3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase

comment:
The enzyme also catalyses the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent.

reaction:
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine


entry: 2.8.2.9
sysname: 3'-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase
comment: Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1 aryl sulfotransferase).
iubmb_reaction: R04213
name:
--- 
- tyrosine-ester sulfotransferase
- aryl sulfotransferase IV
- L-tyrosine methyl ester sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate [RN:R04213]


entry: 2.8.2.10
sysname: 3'-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase
comment: The product may be identical with Watasenia luciferin.
iubmb_reaction: R03138
name:
--- 
- Renilla-luciferin sulfotransferase
- luciferin sulfotransferase
- luciferin sulfokinase
- luciferin sulfokinase (3'-phosphoadenylyl sulfate:luciferin sulfotransferase)

reaction:
3'-phosphoadenylyl sulfate + Renilla luciferin = adenosine 3',5'-bisphosphate + luciferyl sulfate [RN:R03138]


entry: 2.8.2.11
sysname: 3'-phosphoadenylyl-sulfate:galactosylceramide 3'-sulfotransferase
comment: Also acts on lactosylceramide.
iubmb_reaction: R04017 R06279(G)
kegg_reaction: R05105 R06122(G)
name:
--- 
- galactosylceramide sulfotransferase
- GSase
- 3'-phosphoadenosine-5'-phosphosulfate-cerebroside sulfotransferase
- galactocerebroside sulfotransferase
- galactolipid sulfotransferase
- glycolipid sulfotransferase
- glycosphingolipid sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + galactosylceramidesulfate [RN:R04017 R06279]


entry: 2.8.2.12
name: --- - Deleted entry
comment:
Deleted entry: heparitin sulfotransferase. Enzyme identical to EC 2.8.2.8, [heparan sulfate]-glucosamine N-sulfotransferase (EC 2.8.2.12 created 1972, deleted 2001)


entry: 2.8.2.13
sysname: 3'-phosphoadenylyl-sulfate:galactosylsphingosine sulfotransferase
iubmb_reaction: R03700
name:
--- 
- psychosine sulfotransferase
- PAPS:psychosine sulphotransferase
- 3'-phosphoadenosine 5'-phosphosulfate-psychosine sulphotransferase

reaction:
3'-phosphoadenylyl sulfate + galactosylsphingosine = adenosine 3',5'-bisphosphate + psychosine sulfate [RN:R03700]


entry: 2.8.2.14
sysname: 3'-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase
iubmb_reaction: R07287 R03987
name:
--- 
- bile-salt sulfotransferase
- BAST I
- bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase
- bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase
- bile acid sulfotransferase I
- glycolithocholate sulfotransferase

comment:
The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5beta-bile acid glycolithocholate, deoxycholate, 3beta-hydroxy-5-cholenoate and dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3].

reaction:
(1) 3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate [RN:R07287]; (2) 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate [RN:R03987]


entry: 2.8.2.15
name: --- - steroid sulfotransferase - steroid alcohol sulfotransferase
sysname: 3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase
comment: Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone.
iubmb_reaction: R03946 > R00535 R00536 R00537 R02350
reaction:
3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate [RN:R03946]


entry: 2.8.2.16
sysname: 3'-phosphoadenylyl-sulfate:thiol S-sulfotransferase
comment: Also acts on dithiols; substrates include glutathione, dithioerythritol and 2,3-mercaptopropanol.
iubmb_reaction: R01236
name:
--- 
- thiol sulfotransferase
- phosphoadenylylsulfate-thiol sulfotransferase
- PAPS sulfotransferase
- adenosine 3'-phosphate 5'-sulphatophosphate sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate [RN:R01236]


entry: 2.8.2.17
sysname: 3'-phosphoadenylyl-sulfate:chondroitin 6'-sulfotransferase
iubmb_reaction: R02181
name:
--- 
- chondroitin 6-sulfotransferase
- chondroitin 6-O-sulfotransferase
- 3'-phosphoadenosine 5'-phosphosulfate (PAPS):chondroitin sulfate sulfotransferase
- terminal 6-sulfotransferase

comment:
The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin. Not identical with EC 2.8.2.5 chondroitin 4-sulfotransferase.

reaction:
3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]


entry: 2.8.2.18
sysname: 3'-phosphoadenylyl-sulfate:cortisol 21-sulfotransferase
iubmb_reaction: R02839
name:
--- 
- cortisol sulfotransferase
- glucocorticosteroid sulfotransferase
- glucocorticoid sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + cortisol = adenosine 3',5'-bisphosphate + cortisol 21-sulfate [RN:R02839]


entry: 2.8.2.19
sysname: 3'-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol 6-sulfotransferase
iubmb_reaction: R04643
name:
--- 
- triglucosylalkylacylglycerol sulfotransferase
- triglucosylmonoalkylmonoacyl sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,3-1-O- alkyl-2-O-acylglycerol = adenosine 3',5'-bisphosphate + 6-sulfo-alpha-D-glucosyl-1,6-alpha-D-glucosyl-1,6-alpha-D-glucosyl- 1,3-1-O-alkyl-2-O-acylglycerol [RN:R04643]


entry: 2.8.2.20
name: --- - protein-tyrosine sulfotransferase - tyrosylprotein sulfotransferase
sysname: 3'-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase
comment: The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.
iubmb_reaction: R02586
reaction:
3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586]


entry: 2.8.2.21
sysname: 3'-phosphoadenylyl-sulfate:keratan 6'-sulfotransferase
iubmb_reaction: R03553
name:
--- 
- keratan sulfotransferase
- 3'-phosphoadenylyl keratan sulfotransferase
- keratan sulfate sulfotransferase
- 3'-phosphoadenylylsulfate:keratan sulfotransferase

comment:
Sulfation takes place at the 6-position of galactosyl and N-acetylglucosaminyl residues in keratan, a proteoglycan. Not identical with EC 2.8.2.5 (chondroitin 4-sulfotransferase), EC 2.8.2.6 (choline sulfotransferase) or EC 2.8.2.17 (chondroitin 6-sulfotransferase).

reaction:
3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate [RN:R03553]


entry: 2.8.2.22
sysname: aryl-sulfate:phenol sulfotransferase
reaction: an aryl sulfate + a phenol = a phenol + an aryl sulfate
iubmb_reaction: (other) R02996
kegg_reaction: R02996
name:
--- 
- aryl-sulfate sulfotransferase
- arylsulfate-phenol sulfotransferase
- arylsulfotransferase
- ASST
- arylsulfate sulfotransferase
- arylsulfate:phenol sulfotransferase

comment:
Hydroxy groups of tyrosine residues in peptides such as angiotensin can act as acceptors. Does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate.


entry: 2.8.2.23
sysname: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
iubmb_reaction: (other) R04064
kegg_reaction: R04064
name:
--- 
- "[heparan sulfate]-glucosamine 3-sulfotransferase 1"
- heparin-glucosamine 3-O-sulfotransferase
- 3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase
- glucosaminyl 3-O-sulfotransferase
- heparan sulfate D-glucosaminyl 3-O-sulfotransferase
- isoform/isozyme 1 (3-OST-1, HS3ST1)

comment:
This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3)] by being the most selective for a precursor of the antithrombin-binding site. It has a minimal acceptor sequence of: -> GlcNAc6S-> GlcA-> GlcN2S*+/-6S-> IdoA2S-> GlcN2S-> , the asterisk marking the target (symbols as in 2-Carb-38 using +/- to mean the presence or absence of a substituent, and > to separate a predominant structure from a minor one. Thus Glc(N2S > NAc) means a residue of glucosamine where the N carries a sulfo group mainly but occasionally an acetyl group.) [1-4]. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. These precursors are variants of the consensus sequence: -> Glc(N2S > NAc)+/-6S-> GlcA-> GlcN2S*+/-6S-> GlcA > IdoA+/-2S-> Glc(N2S/NAc)+/-6S-> [5]. If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA [6].

reaction:
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate


entry: 2.8.2.24
sysname: 3'-phosphoadenylyl-sulfate:desulfoglucosinolate sulfotransferase
iubmb_reaction: R03214
name:
--- 
- desulfoglucosinolate sulfotransferase
- PAPS-desulfoglucosinolate sulfotransferase
- 3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate sulfotransferase

comment:
Involved with EC 2.4.1.195 thiohydroximate beta-D-glucosyltransferase, in the biosynthesis of thioglycosides in cruciferous plants.

reaction:
3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin [RN:R03214]


entry: 2.8.2.25
name: --- - flavonol 3-sulfotransferase
sysname: 3'-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase
comment: Also acts on some other flavonol aglycones.
iubmb_reaction: R02159
reaction:
3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate [RN:R02159]


entry: 2.8.2.26
sysname: 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 3'-sulfotransferase
iubmb_reaction: R02632
name:
--- 
- quercetin-3-sulfate 3'-sulfotransferase
- flavonol 3'-sulfotransferase
- 3'-Sulfotransferase
- PAPS:flavonol 3-sulfate 3'-sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,3'-bissulfate [RN:R02632]


entry: 2.8.2.27
sysname: 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 4'-sulfotransferase
iubmb_reaction: R02633
name:
--- 
- quercetin-3-sulfate 4'-sulfotransferase
- flavonol 4'-sulfotransferase
- PAPS:flavonol 3-sulfate 4'-sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,4'-bissulfate [RN:R02633]


entry: 2.8.2.28
sysname: 3'-phosphoadenylyl-sulfate:quercetin-3,3'-bissulfate 7-sulfotransferase
comment: Quercetin 3,4'-bissulfate can also act as acceptor.
iubmb_reaction: R03289
kegg_reaction: R06809
name:
--- 
- quercetin-3,3'-bissulfate 7-sulfotransferase
- flavonol 7-sulfotransferase
- 7-sulfotransferase
- PAPS:flavonol 3,3'/3,4'-disulfate 7-sulfotransferase

reaction:
3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate = adenosine 3',5'-bisphosphate + quercetin 3,7,3'-trissulfate [RN:R03289]


entry: 2.8.2.29
sysname: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
iubmb_reaction: R05798
name:
--- 
- "[heparan sulfate]-glucosamine 3-sulfotransferase 2"
- glucosaminyl 3-O-sulfotransferase
- heparan sulfate D-glucosaminyl 3-O-sulfotransferase
- isoform/isozyme 2 (3-OST-2, HS3ST2)

comment:
This enzyme sulfates the residues marked with an asterisk in sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S-> GlcN*-> (symbols as in 2-Carb-38). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.

reaction:
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]


entry: 2.8.2.30
sysname: 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
iubmb_reaction: R05798
name:
--- 
- "[heparan sulfate]-glucosamine 3-sulfotransferase 3"
- glucosaminyl 3-O-sulfotransferase 3a, 3b
- heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A
- isoform/isozyme 3a and 3b (3-OST-3A, 3-OST-3B, HS3ST3A, HS3ST3B)

comment:
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].

reaction:
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]


entry: 2.8.2.31
name: --- - petromyzonol sulfotransferase - PZ-SULT
sysname: 3'-phosphoadenylyl-sulfate:5alpha-cholan-3alpha,7alpha,12alpha,24-te trol sulfotransferase
comment:
The enzyme from the lamprey Petromyzon marinus can also use the corresponding 3-ketone as a substrate. It is stereoselective (5alpha-cholane) and regioselective, exhibiting a preference for an hydroxy group at C-24. The enzyme is inactive when allocholic acid, which has a carboxy group at C-24, is used as a substrate.

reaction:
3'-phosphoadenylyl sulfate + 5alpha-cholan-3alpha,7alpha,12alpha,24-tetrol = adenosine 3',5'-bisphosphate + 5alpha-cholan-3alpha,7alpha,12alpha-triol 24-sulfate


entry: 2.8.2.32
name: --- - scymnol sulfotransferase
sysname: 3'-phosphoadenosine 5'-phosphosulfate:5beta-scymnol sulfotransferase
comment:
The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C27 bile salts 5beta-scymnol (the natural bile salt) and 5alpha-cyprinol (the carp bile salt). Enzyme activity is activated by Mg2+ but inhibited by the product 5beta-scymnol sulfate.

reaction:
3'-phosphoadenosine 5'-phosphosulfate + 5beta-scymnol = adenosine 3',5'-bisphosphate + 5beta-scymnol sulfate


entry: 2.8.2.33
name: --- - N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase - GalNAc4S-6ST
sysname: 3'-phosphoadenylyl-sulfate:dermatan 6'-sulfotransferase
iubmb_reaction: R07288 R02181
comment:
The enzyme is activated by divalent cations and reduced glutathione. The enzyme from human transfers sulfate to position 6 of both internal residues and nonreducing terminal GalNAc 4-sulfate residues of chondroitin sulfate. Oligosaccharides derived from chondroitin sulfate also serve as acceptors but chondroitin sulfate E, keratan sulfate and heparan sulfate do not. Differs from EC 2.8.2.17, chondroitin 6-sulfotransferase, in being able to use both condoitin and dermatan as effective substrates

reaction:
(1) 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate [RN:R07288]; (2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]


entry: 2.8.2.34
sysname: 3'-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase
iubmb_reaction: R07289
name:
--- 
- glycochenodeoxycholate sulfotransferase
- bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase
- bile acid:PAPS:sulfotransferase
- BAST

comment:
The enzyme specifically sulfates glycochenodeoxycholate at the 7alpha-position (see also EC 2.8.2.14 bile-salt sulfotransferase). The monohydroxy bile acids glycolithocholate, chenodeoxycholate and ursodeoxycholate act as inhibitors.

reaction:
3'-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate [RN:R07289]


entry: 2.8.2.-
name: --- []
reaction:
2-Aminoacrylate + 3'-Phosphoadenylyl sulfate <=> L-Cysteate + Adenosine 3',5'-bisphosphate [RN:R02435]


entry: 2.8.3.1
sysname: acetyl-CoA:propanoate CoA-transferase
comment: Butanoate and lactate can also act as acceptors.
reaction: acetyl-CoA + propanoate = acetate + propanoyl-CoA [RN:R00928]
iubmb_reaction: R00928
kegg_reaction: R01449 R05508
name:
--- 
- propionate CoA-transferase
- propionate coenzyme A-transferase
- propionate-CoA:lactoyl-CoA transferase
- propionyl CoA:acetate CoA transferase
- propionyl-CoA transferase


entry: 2.8.3.2
sysname: succinyl-CoA:oxalate CoA-transferase
reaction: succinyl-CoA + oxalate = succinate + oxalyl-CoA [RN:R01559]
iubmb_reaction: R01559
name:
--- 
- oxalate CoA-transferase
- succinyl-beta-ketoacyl-CoA transferase
- oxalate coenzyme A-transferase


entry: 2.8.3.3
name: --- - malonate CoA-transferase - malonate coenzyme A-transferase
sysname: acetyl-CoA:malonate CoA-transferase
reaction: acetyl-CoA + malonate = acetate + malonyl-CoA [RN:R00743]
iubmb_reaction: R00743
comment:
The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 4.1.1.9 malonyl-CoA decarboxylase.


entry: 2.8.3.5
sysname: succinyl-CoA:3-oxo-acid CoA-transferase
reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA [RN:R01780]
iubmb_reaction: R01780 > R00410
name:
--- 
- 3-oxoacid CoA-transferase
- 3-oxoacid coenzyme A-transferase
- 3-ketoacid CoA-transferase
- 3-ketoacid coenzyme A transferase
- 3-oxo-CoA transferase
- 3-oxoacid CoA dehydrogenase
- acetoacetate succinyl-CoA transferase
- acetoacetyl coenzyme A-succinic thiophorase
- succinyl coenzyme A-acetoacetyl coenzyme A-transferase
- succinyl-CoA transferase

comment:
Acetoacetate and, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptors; malonyl-CoA can act instead of succinyl-CoA.


entry: 2.8.3.6
sysname: succinyl-CoA:3-oxoadipate CoA-transferase
reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA [RN:R02990]
iubmb_reaction: R02990
name:
--- 
- 3-oxoadipate CoA-transferase
- 3-oxoadipate coenzyme A-transferase
- 3-oxoadipate succinyl-CoA transferase


entry: 2.8.3.7
sysname: succinyl-CoA:citramalate CoA-transferase
comment: Itaconate can also act as acceptor.
reaction: succinyl-CoA + citramalate = succinate + citramalyl-CoA [RN:R02956]
iubmb_reaction: R02956 > R03154
kegg_reaction: R02407
name:
--- 
- succinate-citramalate CoA-transferase
- itaconate CoA-transferase
- citramalate CoA-transferase
- citramalate coenzyme A-transferase
- succinyl coenzyme A-citramalyl coenzyme A transferase


entry: 2.8.3.8
sysname: acyl-CoA:acetate CoA-transferase
comment: Acts on butanoyl-CoA and pentanoyl-CoA.
reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA [RN:R00393]
iubmb_reaction: R00393 > R01179 R01359
name:
--- 
- acetate CoA-transferase
- acetate coenzyme A-transferase
- butyryl CoA:acetate CoA transferase
- butyryl coenzyme A transferase
- succinyl-CoA:acetate CoA transferase


entry: 2.8.3.9
sysname: butanoyl-CoA:acetoacetate CoA-transferase
reaction: butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA [RN:R01365]
iubmb_reaction: R01365
name:
--- 
- butyrate-acetoacetate CoA-transferase
- butyryl coenzyme A-acetoacetate coenzyme A-transferase
- butyryl-CoA-acetoacetate CoA-transferase

comment:
Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids.


entry: 2.8.3.10
name: --- - citrate CoA-transferase
sysname: acetyl-CoA:citrate CoA-transferase
reaction: acetyl-CoA + citrate = acetate + (3S)-citryl-CoA [RN:R01323]
iubmb_reaction: R01323
comment:
The enzyme is a component of EC 4.1.3.6 [citrate (pro-3S)-lyase]. Also catalyses the transfer of thioacyl carrier protein from its acetyl thioester to citrate.


entry: 2.8.3.11
name: --- - citramalate CoA-transferase
sysname: acetyl-CoA:citramalate CoA-transferase
reaction: acetyl-CoA + citramalate = acetate + (3S)-citramalyl-CoA [RN:R02955]
iubmb_reaction: R02955 > R03153
comment:
The enzyme is a component of EC 4.1.3.22 citramalate lyase. Also catalyses the transfer of thioacyl carrier protein from its acetyl thioester to citramalate.


entry: 2.8.3.12
name: --- - glutaconate CoA-transferase
sysname: acetyl-CoA:(E)-glutaconate CoA-transferase
reaction: acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA [RN:R03884]
iubmb_reaction: R03884
kegg_reaction: R04000 R05509
comment:
Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but not (Z)-glutaconate, can also act as acceptors.


entry: 2.8.3.13
sysname: succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase
comment: Malonyl-CoA can also act as donor, but more slowly.
iubmb_reaction: R02084
name:
--- 
- succinate-hydroxymethylglutarate CoA-transferase
- hydroxymethylglutarate coenzyme A-transferase
- dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase

reaction:
succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + (S)-3-hydroxy-3-methylglutaryl-CoA [RN:R02084]


entry: 2.8.3.14
sysname: acetyl-CoA:5-hydroxypentanoate CoA-transferase
reaction: acetyl-CoA + 5-hydroxypentanoate = acetate + 5-hydroxypentanoyl-CoA [RN:R04057]
iubmb_reaction: R04057
name:
--- 
- 5-hydroxypentanoate CoA-transferase
- 5-hydroxyvalerate CoA-transferase
- 5-hydroxyvalerate coenzyme A transferase

comment:
Propanoyl-CoA, acetyl-CoA, butanoyl-CoA and some other acyl-CoAs can act as substrates, but more slowly than 5-hydroxypentanoyl-CoA.


entry: 2.8.3.15
name: --- - succinyl-CoA:(R)-benzylsuccinate CoA-transferase - benzylsuccinate CoA-transferase
sysname: succinyl-CoA:(R)-2-benzylsuccinate CoA-transferase
reaction: succinyl-CoA + (R)-2-benzylsuccinate = succinate + (R)-2-benzylsuccinyl-CoA [RN:R05588]
iubmb_reaction: R05588
comment:
Involved in anaerobic catabolism of toluene and is a strictly toluene-induced enzyme that catalyses the reversible regio- and enantio-selective synthesis of (R)-2-benzylsuccinyl-CoA. The enzyme from Thauera aromatica is inactive when (R)-benzylsuccinate is replaced by (S)-benzylsuccinate.


entry: 2.8.3.16
name: --- - formyl-CoA transferase - formyl-coenzyme A transferase - formyl-CoA oxalate CoA-transferase
sysname: formyl-CoA:oxalate CoA-transferase
reaction: formyl-CoA + oxalate = formate + oxalyl-CoA [RN:R07290]
iubmb_reaction: R07290
comment:
The enzyme from Oxalobacter formigenes can also catalyse the transfer of CoA from formyl-CoA to succinate.


entry: 2.8.3.17
name: --- - cinnamoyl-CoA:phenyllactate CoA-transferase - FldA
sysname: (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase
reaction: (E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate + (R)-phenyllactyl-CoA
comment:
3-Phenylproprionate is a better CoA acceptor than (R)-phenyllactate in vitro. The enzyme from Clostridium sporogenes is specific for derivatives of 3-phenylpropionate and 4-phenylbutyrate.


entry: 2.8.3.-
name: --- []
reaction:
Naphthyl-2-methyl-succinic acid + Succinyl-CoA <=> Naphthyl-2-methyl-succinyl-CoA + Succinate [RN:R06904]


entry: 2.8.4.1
name: --- - coenzyme-B sulfoethylthiotransferase - methyl-CoM reductase - methyl coenzyme M reductase
iubmb_reaction: R04541
sysname:
2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreoni ne S-(2-sulfoethyl)thiotransferase

comment:
The enzyme from methanogenic bacteria requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen.

reaction:
2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM-S-S-CoB + methane [RN:R04541]


entry: 2.9.1.1
sysname: selenophosphate:L-seryl-tRNA(Sec) selenium transferase
reaction: L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + H2O + phosphate
iubmb_reaction: (other) R04689
kegg_reaction: R04689
name:
--- 
- L-seryl-tRNA(Sec) selenium transferase
- L-selenocysteinyl-tRNA(Sel) synthase
- L-selenocysteinyl-tRNA(Sec) synthase selenocysteine synthase
- cysteinyl-tRNA(Sec)-selenium transferase

comment:
a pyridoxal 5'-phosphate enzyme identified in Escherichia coli. Recognises specifically tRNA(Sec)-species. Binding of tRNA(Sec) also occurs in the absence of the seryl group. 2-Aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction. Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNA(Sec). The symbol Sel has also been used for selenocysteine but Sec is preferred.


entry: 2.-.-.-
name: --- []
reaction:
(1) 2,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D- glucosamine 1,4'-bisphosphate + CMP-3-deoxy-D-manno-octulosonate <=> 3-Deoxy-D-manno-octulosonyl-lipid IV(A) + CMP [RN:R04658]; (2) 3-Deoxy-D-manno-octulosonyl-lipid IV(A) + CMP-3-deoxy-D-manno-octulosonate <=> Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) + CMP [RN:R05074 R06285]


entry: 3.1.1.1
sysname: carboxylic-ester hydrolase
reaction: A carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
iubmb_reaction: R00630 > R06728
name:
--- 
- carboxylesterase
- ali-esterase
- B-esterase
- monobutyrase
- cocaine esterase
- procaine esterase
- methylbutyrase
- vitamin A esterase
- butyryl esterase
- carboxyesterase
- carboxylate esterase
- carboxylic esterase
- methylbutyrate esterase
- triacetin esterase
- carboxyl ester hydrolase
- butyrate esterase
- alpha-carboxylesterase
- propionyl esterase
- nonspecific carboxylesterase
- esterase D
- esterase B
- esterase A
- serine esterase
- carboxylic acid esterase

comment:
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.


entry: 3.1.1.2
name: --- - arylesterase - A-esterase - paraoxonase - aromatic esterase
sysname: aryl-ester hydrolase
reaction: a phenyl acetate + H2O = a phenol + acetate [RN:R07342]
iubmb_reaction: R07342 > R01241 R06893
comment:
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [8].


entry: 3.1.1.3
sysname: triacylglycerol acylhydrolase
reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
iubmb_reaction: R01369 > R02250
kegg_reaction: R02687 R02688 R05209
name:
--- 
- triacylglycerol lipase
- lipase
- triglyceride lipase
- tributyrase
- butyrinase
- glycerol ester hydrolase
- tributyrinase
- Tween hydrolase
- steapsin
- triacetinase
- tributyrin esterase
- Tweenase
- amno N-AP
- Takedo 1969-4-9
- Meito MY 30
- Tweenesterase
- GA 56
- capalase L
- triglyceride hydrolase
- triolein hydrolase
- tween-hydrolyzing esterase
- amano CE
- cacordase
- triglyceridase
- triacylglycerol ester hydrolase
- amano P
- amano AP
- PPL
- glycerol-ester hydrolase
- GEH
- meito Sangyo OF lipase
- hepatic lipase
- lipazin
- post-heparin plasma protamine-resistant lipase
- salt-resistant post-heparin lipase
- heparin releasable hepatic lipase
- amano CES
- amano B
- liver lipase
- hepatic monoacylglycerol acyltransferase

comment:
The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolysed.


entry: 3.1.1.4
name: --- - phospholipase A2 - lecithinase A - phosphatidase - phosphatidolipase - phospholipase A
sysname: phosphatidylcholine 2-acylhydrolase
reaction: phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
iubmb_reaction: R01313
kegg_reaction: R01315 R01317 R02053 R03107 R07064 R07291 R07379 R07387
comment:
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.


entry: 3.1.1.5
sysname: 2-lysophosphatidylcholine acylhydrolase
reaction: 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
iubmb_reaction: (other) R01309 R02744 R02746 R02747 R03416 R03417 R04499
kegg_reaction: R01309 R02744 R02746 R02747 R03416 R03417 R04499
name:
--- 
- lysophospholipase
- lecithinase B
- lysolecithinase
- phospholipase B
- lysophosphatidase
- lecitholipase
- phosphatidase B
- lysophosphatidylcholine hydrolase
- lysophospholipase A1
- lysophopholipase L2
- "lysophospholipase\xD0transacylase"
- neuropathy target esterase
- NTE
- NTE-LysoPLA
- NTE-lysophospholipase


entry: 3.1.1.6
sysname: acetic-ester acetylhydrolase
reaction: An acetic ester + H2O = an alcohol + acetate
iubmb_reaction: (other) R00628
kegg_reaction: R00628
name:
--- 
- acetylesterase
- C-esterase (in animal tissues)
- acetic ester hydrolase
- chloroesterase
- p-nitrophenyl acetate esterase
- Citrus acetylesterase


entry: 3.1.1.7
sysname: acetylcholine acetylhydrolase
comment: Acts on a variety of acetic esters; also catalyses transacetylations.
reaction: acetylcholine + H2O = choline + acetate [RN:R01026]
iubmb_reaction: R01026
name:
--- 
- acetylcholinesterase
- true cholinesterase
- choline esterase I
- cholinesterase
- acetylthiocholinesterase
- acetylcholine hydrolase
- acetyl.beta-methylcholinesterase
- AcCholE


entry: 3.1.1.8
sysname: acylcholine acylhydrolase
comment: Acts on a variety of choline esters and a few other compounds.
reaction: An acylcholine + H2O = choline + a carboxylate
iubmb_reaction: (other) R01029
kegg_reaction: R01029
name:
--- 
- cholinesterase
- pseudocholinesterase
- butyrylcholine esterase
- non-specific cholinesterase
- choline esterase II (unspecific)
- benzoylcholinesterase
- choline esterase
- butyrylcholinesterase
- propionylcholinesterase
- anticholineesterase
- BtChoEase


entry: 3.1.1.9
name: --- - Deleted entry
comment:
Deleted entry: benzoylcholinesterase; a side reaction of EC 3.1.1.8 cholinesterase (EC 3.1.1.9 created 1961, deleted 1972)


entry: 3.1.1.11
sysname: pectin pectylhydrolase
reaction: pectin + n H2O = n methanol + pectate [RN:R02362 R06250]
iubmb_reaction: R02362 R06250(G)
name:
--- 
- pectinesterase
- pectin demethoxylase
- pectin methoxylase
- pectin methylesterase
- pectase
- pectin methyl esterase
- pectinoesterase


entry: 3.1.1.12
name: --- - Deleted entry
comment:
Deleted entry: vitamin A esterase, now believed to be identical with EC 3.1.1.1 carboxylesterase (EC 3.1.1.12 created 1961, deleted 1972)


entry: 3.1.1.13
sysname: steryl-ester acylhydrolase
reaction: A steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
iubmb_reaction: R02115 > R01462
name:
--- 
- sterol esterase
- cholesterol esterase
- cholesteryl ester synthase
- triterpenol esterase
- cholesteryl esterase
- cholesteryl ester hydrolase
- sterol ester hydrolase
- cholesterol ester hydrolase
- cholesterase
- acylcholesterol lipase

comment:
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.


entry: 3.1.1.16
name: --- - Deleted entry
comment:
Deleted entry: 4-carboxymethyl-4-hydroxyisocrotonolactonase. This reaction was due to a mixture of EC 5.3.3.4 (muconolactone D-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase) (EC 3.1.1.16 created 1961, deleted 1972)


entry: 3.1.1.17
name: --- - gluconolactonase - lactonase - aldonolactonase - glucono-delta-lactonase - gulonolactonase
sysname: D-glucono-1,5-lactone lactonohydrolase
reaction: D-glucono-1,5-lactone + H2O = D-gluconate [RN:R01519]
iubmb_reaction: R01519
kegg_reaction: R02525 R02933 R03751 R04785
comment:
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed as EC 3.1.1.18, aldonolactonase.


entry: 3.1.1.18
name: --- - Deleted entry
comment:
Deleted entry: aldonolactonase. Now included with EC 3.1.1.17 gluconolactonase (EC 3.1.1.18 created 1961, deleted 1982)


entry: 3.1.1.21
sysname: retinyl-palmitate palmitohydrolase
reaction: retinyl palmitate + H2O = retinol + palmitate [RN:R02368]
iubmb_reaction: R02368
name:
--- 
- retinyl-palmitate esterase
- retinyl palmitate hydrolase
- retinyl palmitate hydrolyase
- retinyl ester hydrolase


entry: 3.1.1.23
sysname: glycerol-ester acylhydrolase
reaction: Hydrolyses glycerol monoesters of long-chain fatty acids
iubmb_reaction: (other) R01351 R01352
kegg_reaction: R01351 R01352
name:
--- 
- acylglycerol lipase
- monoacylglycerol lipase
- monoacylglycerolipase
- monoglyceride lipase
- monoglyceride hydrolase
- fatty acyl monoester lipase
- monoacylglycerol hydrolase
- monoglyceridyllipase
- monoglyceridase


entry: 3.1.1.24
sysname: 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
comment: The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
reaction: 3-oxoadipate enol-lactone + H2O = 3-oxoadipate [RN:R02991]
iubmb_reaction: R02991
name:
--- 
- 3-oxoadipate enol-lactonase
- carboxymethylbutenolide lactonase
- beta-ketoadipic enol-lactone hydrolase
- 3-ketoadipate enol-lactonase
- 3-oxoadipic enol-lactone hydrolase
- beta-ketoadipate enol-lactone hydrolase


entry: 3.1.1.25
name: --- - 1,4-lactonase - gamma-lactonase
sysname: 1,4-lactone hydroxyacylhydrolase
reaction: A 1,4-lactone + H2O = a 4-hydroxyacid [RN:R03708]
iubmb_reaction: R03708 > R02933 R03034
comment:
The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.


entry: 3.1.1.26
name: --- - galactolipase - galactolipid lipase - polygalactolipase - galactolipid acylhydrolase
sysname: 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol acylhydrolase
iubmb_reaction: R03467
kegg_reaction: R04471
comment:
Also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glyce rol, and phosphatidylcholine and other phospholipids.

reaction:
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates [RN:R03467]


entry: 3.1.1.28
sysname: O-acylcarnitine acylhydrolase
reaction: O-acylcarnitine + H2O = a fatty acid + L-carnitine [RN:R01924]
iubmb_reaction: R01924
name:
--- 
- acylcarnitine hydrolase
- high activity acylcarnitine hydrolase
- HACH
- carnitine ester hydrolase
- palmitoylcarnitine hydrolase
- palmitoyl-L-carnitine hydrolase
- long-chain acyl-L-carnitine hydrolase
- palmitoyl carnitine hydrolase

comment:
Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine.


entry: 3.1.1.29
sysname: aminoacyl-tRNA aminoacylhydrolase
reaction: N-Substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA [RN:R04238]
iubmb_reaction: R04238
name:
--- 
- aminoacyl-tRNA hydrolase
- aminoacyl-transfer ribonucleate hydrolase
- N-substituted aminoacyl transfer RNA hydrolase
- peptidyl-tRNA hydrolase


entry: 3.1.1.34
sysname: triacylglycero-protein acylhydrolase
reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
iubmb_reaction: R01369
kegg_reaction: R01350
name:
--- 
- lipoprotein lipase
- clearing factor lipase
- diglyceride lipase
- diacylglycerol lipase
- postheparin esterase
- postheparin lipase
- diacylglycerol hydrolase
- lipemia-clearing factor

comment:
Hydrolyses triacylglycerols in chylomicrons and low-density lipoproteins. Also hydrolyses diacylglycerol.


entry: 3.1.1.38
sysname: triacetolactone lactonohydrolase
reaction: triacetate lactone + H2O = triacetate [RN:R03702]
iubmb_reaction: R03702
name:
--- 
- triacetate-lactonase
- triacetic lactone hydrolase
- triacetic acid lactone hydrolase
- TAL hydrolase
- triacetate lactone hydrolase


entry: 3.1.1.40
name: --- - orsellinate-depside hydrolase - lecanorate hydrolase
sysname: orsellinate-depside hydrolase
reaction: orsellinate depside + H2O = 2 orsellinate [RN:R00054]
iubmb_reaction: R00054
comment:
The enzyme will only hydrolyse those substrates based on the 2,4-dihydroxy-6-methylbenzoate structure that also have a free hydroxy group ortho to the depside linkage.


entry: 3.1.1.41
sysname: cephalosporin-C acetylhydrolase
comment: Hydrolyses the acetyl ester bond on the 10-position of the antibiotic cephalosporin C.
reaction: cephalosporin C + H2O = deacetylcephalosporin C + acetate [RN:R03062]
iubmb_reaction: R03062
name:
--- 
- cephalosporin-C deacetylase
- cephalosporin C acetyl-hydrolase
- cephalosporin C acetylase
- cephalosporin acetylesterase
- cephalosporin C acetylesterase
- cephalosporin C acetyl-esterase
- cephalosporin C deacetylase


entry: 3.1.1.45
sysname: 4-carboxymethylenebut-2-en-4-olide lactonohydrolase
reaction: 4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate [RN:R03893]
iubmb_reaction: R03893
kegg_reaction: R05510 R05511 R06835 R06838
name:
--- 
- carboxymethylenebutenolidase
- maleylacetate enol-lactonase
- dienelactone hydrolase
- carboxymethylene butenolide hydrolase


entry: 3.1.1.46
name: --- - deoxylimonate A-ring-lactonase
sysname: deoxylimonate A-ring-lactonohydrolase
reaction: deoxylimonate + H2O = deoxylimononic acid D-ring-lactone [RN:R03803]
iubmb_reaction: R03803
comment:
The enzyme opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the D-ring-lactone intact.


entry: 3.1.1.47
sysname: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
iubmb_reaction: R04452
name:
--- 
- 1-alkyl-2-acetylglycerophosphocholine esterase
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase
- alkylacetyl-GPC:acetylhydrolase

reaction:
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]


entry: 3.1.1.48
name: --- - fusarinine-C ornithinesterase - ornithine esterase
sysname: N5-acyl-L-ornithine-ester hydrolase
reaction: N5-acyl-L-ornithine ester + H2O = N5-acyl-L-ornithine + an alcohol [RN:R04070]
iubmb_reaction: R04070
comment:
Hydrolyses the three ornithine ester bonds in fusarinine C. Also acts on N5-dinitrophenyl-L-ornithine methyl ester.


entry: 3.1.1.51
sysname: 12,13-diacylphorbate 12-acylhydrolase
reaction: phorbol 12,13-dibutanoate + H2O = phorbol 13-butanoate + butanoate [RN:R04119]
iubmb_reaction: R04119
name:
--- 
- phorbol-diester hydrolase
- diacylphorbate 12-hydrolase
- phorbol-12,13-diester 12-ester hydrolase
- PDEH

comment:
Hydrolyses the 12-ester bond in a variety of 12,13-diacylphorbols (phorbol is a diterpenoid); this reaction inactivates the tumour promotor 12-O-tetradecanoylphorbol-13-acetate from croton oil.


entry: 3.1.1.53
sysname: N-acyl-O-acetylneuraminate O-acetylhydrolase
reaction: N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate [RN:R01810]
iubmb_reaction: R01810
name:
--- 
- sialate O-acetylesterase
- N-acetylneuraminate acetyltransferase
- sialate 9(4)-O-acetylesterase
- sialidase

comment:
Acts on free and glycosidically bound N-acetyl- or N-glycoloyl-neuraminic acid; acts mainly on the 4-O- and 9-O-acetyl groups. Also acts on some other O-acetyl esters, both cyclic and acyclic compounds, which are not sialic acids.


entry: 3.1.1.54
sysname: 5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene O-acetylhydrolase
comment: The enzyme is highly specific.
iubmb_reaction: R04490
name:
--- 
- acetoxybutynylbithiophene deacetylase
- acetoxybutynylbithiophene esterase
- 5-(4-acetoxy-1-butynyl)-2,2'-bithiophene:acetate esterase

reaction:
5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene + H2O = 5-(4-hydroxybut-1-ynyl)-2,2'-bithiophene + acetate [RN:R04490]


entry: 3.1.1.55
sysname: acetylsalicylate O-acetylhydrolase
reaction: acetylsalicylate + H2O = salicylate + acetate [RN:R02942]
iubmb_reaction: R02942
name:
--- 
- acetylsalicylate deacetylase
- aspirin esterase
- acetylsalicylic acid esterase
- aspirin hydrolase

comment:
Not identical with EC 3.1.1.1 (carboxylesterase), EC 3.1.1.2 (arylesterase), EC 3.1.1.7 (acetylcholinesterase) or EC 3.1.1.8 (cholinesterase). The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolysed; the microsomal enzyme also hydrolyses some other negatively charged esters, with highest activity on esters of salicylate with long-chain alcohols.


entry: 3.1.1.56
name: --- - methylumbelliferyl-acetate deacetylase - esterase D
sysname: 4-methylumbelliferyl-acetate acylhydrolase
reaction: 4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate [RN:R04141]
iubmb_reaction: R04141
comment:
Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters.


entry: 3.1.1.58
sysname: N-acetyl-D-galactosaminoglycan acetylhydrolase
reaction: N-acetyl-D-galactosaminoglycan + H2O = D-galactosaminoglycan + acetate [RN:R04146]
iubmb_reaction: R04146
name:
--- 
- N-acetylgalactosaminoglycan deacetylase
- polysaccharide deacetylase
- Vi-polysaccharide deacetylase
- N-acetyl galactosaminoglycan deacetylase


entry: 3.1.1.59
sysname: methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-die noate acylhydrolase
iubmb_reaction: R04608
name:
--- 
- juvenile-hormone esterase
- JH-esterase
- juvenile hormone analog esterase
- juvenile hormone carboxyesterase

comment:
Demethylates the insect juvenile hormones, JH1 and JH3, but does not hydrolyse the analogous ethyl or isopropyl esters.

reaction:
methyl (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + H2O = (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + methanol [RN:R04608]


entry: 3.1.1.61
sysname: protein-L-glutamate-O5-methyl-ester acylhydrolase
reaction: protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol [RN:R02624]
iubmb_reaction: R02624
name:
--- 
- protein-glutamate methylesterase
- chemotaxis-specific methylesterase
- methyl-accepting chemotaxis protein methyl-esterase
- CheB methylesterase
- methylesterase CheB
- protein methyl-esterase
- protein carboxyl methylesterase
- PME
- protein methylesterase

comment:
Hydrolyses the products of EC 2.1.1.77 (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC 2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80 (protein-glutamate O-methyltransferase) and EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase).


entry: 3.1.1.62
name: --- - Deleted entry
comment:
Deleted entry. Now listed as EC 3.5.1.47 N-acetyldiaminopimelate deacetylase (EC 3.1.1.62 created 1989, deleted 1992)


entry: 3.1.1.65
sysname: L-rhamnono-1,4-lactone lactonohydrolase
reaction: L-rhamnono-1,4-lactone + H2O = L-rhamnonate [RN:R03772]
iubmb_reaction: R03772
name:
--- 
- L-rhamnono-1,4-lactonase
- L-rhamno-gamma-lactonase
- L-rhamnono-gamma-lactonase
- L-rhamnonate dehydratase


entry: 3.1.1.66
sysname: 5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene acetylhydrolase
comment: A highly specific enzyme from Tagetes patula.
iubmb_reaction: R04525
name:
--- 
- 5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene deacetylase
- diacetoxybutynylbithiophene acetate esterase
- 3,4-diacetoxybutinylbithiophene:4-acetate esterase

reaction:
5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene + H2O = 5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2'-bithiophene + acetate [RN:R04525]


entry: 3.1.1.67
name: --- - fatty-acyl-ethyl-ester synthase - FAEES
sysname: long-chain-fatty-acyl-ethyl-ester acylhydrolase
reaction: A long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid + ethanol [RN:R02682]
iubmb_reaction: R02682
comment:
In the reverse reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP. Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, but more slowly.


entry: 3.1.1.69
name: --- - Transferred to 3.5.1.89
comment:
Transferred entry: now EC 3.5.1.89, N-acetylglucosaminylphosphatidylinositol deacetylase. Previously classified erroneously as an enzyme that hydrolysed an ester and not an amide (EC 3.1.1.69 created 1992, deleted 2002)


entry: 3.1.1.70
name: --- - cetraxate benzylesterase
sysname: cetraxate-benzyl-ester benzylhydrolase
reaction: cetraxate benzyl ester + H2O = cetraxate + benzyl alcohol [RN:R03612]
iubmb_reaction: R03612
comment:
Acts on a number of benzyl esters of substituted phenyl propanoates, and on the benzyl esters of phenylalanine and tyrosine.


entry: 3.1.1.71
name: --- - acetylalkylglycerol acetylhydrolase - alkylacetylglycerol acetylhydrolase
sysname: 2-acetyl-1-alkyl-sn-glycerol acetylhydrolase
reaction: 2-acetyl-1-alkyl-sn-glycerol + H2O = 1-alkyl-sn-glycerol + acetate [RN:R04043]
iubmb_reaction: R04043
comment:
hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. The enzyme from Erlich ascites cells is membrane-bound. It differs from lipoprotein lipase (EC 3.1.1.34) since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase.


entry: 3.1.1.72
name: --- - acetylxylan esterase
sysname: acetylxylan esterase
reaction: Deacetylation of xylans and xylo-oligosaccharides
comment:
catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.


entry: 3.1.1.73
sysname: 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase
reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide [RN:R07292]
iubmb_reaction: R07292
name:
--- 
- feruloyl esterase
- ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes
- FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II

comment:
Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.


entry: 3.1.1.74
name: --- - cutinase
sysname: cutin hydrolase
reaction: cutin + H2O = cutin monomers [RN:R05793]
iubmb_reaction: R05793
comment:
Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.


entry: 3.1.1.75
sysname: poly[(R)-3-hydroxybutyrate] hydrolase
iubmb_reaction: R05797
name:
--- 
- poly(3-hydroxybutyrate) depolymerase
- PHB depolymerase
- poly(3HB) depolymerase
- poly[(R)-hydroxyalkanoic acid] depolymerase
- poly(HA) depolymerase
- poly(HA(SCL)) depolymerase
- poly[(R)-3-hydroxybutyrate] hydrolase

comment:
Reaction also occurs with esters of other short-chain-length (C1-C5) hydroxyalkanoic acids (HA). There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline.

reaction:
poly[(R)-3-hydroxybutanoate]n + H2O = poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x; x = 1-5 [RN:R05797]


entry: 3.1.1.76
sysname: poly{oxycarbonyl[(R)-2-pentylethylene]} hydrolase
reaction: Hydrolyses the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to oligomers [RN:R05796]
iubmb_reaction: R05796
name:
--- 
- poly(3-hydroxyoctanoate) depolymerase
- PHO depolymerase, poly(3HO) depolymerase
- poly[(R)-hydroxyalkanoic acid] depolymerase
- poly(HA) depolymerase
- poly(HA(MCL)) depolymerase
- poly[(R)-3-hydroxyoctanoate] hydrolase

comment:
The main product after prolonged incubation is the dimer [3]. Besides hydrolysing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyses other polymers derived from medium-chain-length (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these. It also hydrolyses p-nitrophenyl esters of fatty acids. Polymers of short-chain-length hydroxyalkanoic acids such as poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic acid] are not hydrolysed.


entry: 3.1.1.77
name: --- - acyloxyacyl hydrolase
iubmb_reaction: R05792
comment:
The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, beta-D-GlcN-(1-> 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups.

reaction:
3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid [RN:R05792]


entry: 3.1.1.78
name: --- - polyneuridine-aldehyde esterase - polyneuridine aldehyde esterase - PNAE
sysname: polyneuridine aldehyde hydrolase (decarboxylating)
reaction: polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol [RN:R05825]
iubmb_reaction: R05825
comment:
Following hydrolysis of this indole alkaloid ester the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton. The enzyme also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde).


entry: 3.1.1.79
name: --- - hormone-sensitive lipase - HSL
sysname: diacylglycerol acylhydrolase
iubmb_reaction: R05209 R01369 R07293
comment:
This enzyme is a serine hydrolase. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4], steroid fatty acid esters [5], retinyl esters [6] and p-nitrophenyl esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond [8]. The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.

reaction:
(1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209]; (2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]; (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]


entry: 3.1.1.80
sysname: 17-O-acetylajmaline O-acetylhydrolase
name:
--- 
- acetylajmaline esterase
- acetylajmalan esterase
- AAE
- 2beta(R)-17-O-acetylajmalan:acetylesterase

comment:
This plant enzyme is responsible for the last stages in the biosynthesis of the indole alkaloid ajmaline. The enzyme is highly specific for the substrates 17-O-acetylajmaline and 17-O-acetylnorajmaline as the structurally related acetylated alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and 1,2-dihydroraucaffricine cannot act as substrates [2]. This is a novel member of the GDSL family of serine esterases/lipases.

reaction:
(1) 17-O-acetylajmaline + H2O = ajmaline + acetate; (2) 17-O-acetylnorajmaline + H2O = norajmaline + acetate


entry: 3.1.1.-
name: --- []
reaction:
(1) Poly-beta-hydroxybutyrate + H2O <=> ((R)-3-Hydroxybutanoyl)(n-2) + (R)-3-((R)-3-Hydroxybutanoyloxy)butanoate [RN:R05118]; (2) 4-Sulfolactone + HO- <=> HSO3- + 2-Maleylacetate [RN:R05420]; (3) Ecgonine methyl ester + H2O <=> Ecgonine + Methanol [RN:R06729]


entry: 3.1.2.1
sysname: acetyl-CoA hydrolase
reaction: acetyl-CoA + H2O = CoA + acetate [RN:R00227]
iubmb_reaction: R00227
name:
--- 
- acetyl-CoA hydrolase
- acetyl-CoA deacylase
- acetyl-CoA acylase
- acetyl coenzyme A hydrolase
- acetyl coenzyme A deacylase
- acetyl coenzyme A acylase
- acetyl-CoA thiol esterase


entry: 3.1.2.2
sysname: palmitoyl-CoA hydrolase
comment: Also hydrolyses CoA thioesters of other long-chain fatty acids.
reaction: palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
iubmb_reaction: R01274
name:
--- 
- palmitoyl-CoA hydrolase
- long-chain fatty-acyl-CoA hydrolase
- palmitoyl coenzyme A hydrolase
- palmitoyl thioesterase
- palmitoyl-CoA deacylase
- palmityl thioesterase
- palmityl-CoA deacylase
- fatty acyl thioesterase I
- palmityl thioesterase I


entry: 3.1.2.3
sysname: succinyl-CoA hydrolase
reaction: succinyl-CoA + H2O = CoA + succinate [RN:R00407]
iubmb_reaction: R00407
name:
--- 
- succinyl-CoA hydrolase
- succinyl-CoA acylase
- succinyl coenzyme A hydrolase
- succinyl coenzyme A deacylase


entry: 3.1.2.5
sysname: (S)-3-hydroxy-3-methylglutaryl-CoA hydrolase
reaction: (S)-3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate [RN:R02083]
iubmb_reaction: R02083
name:
--- 
- hydroxymethylglutaryl-CoA hydrolase
- beta-hydroxy-beta-methylglutaryl coenzyme A hydrolase
- beta-hydroxy-beta-methylglutaryl coenzyme A deacylase
- hydroxymethylglutaryl coenzyme A hydrolase
- hydroxymethylglutaryl coenzyme A deacylase
- 3-hydroxy-3-methylglutaryl-CoA hydrolase


entry: 3.1.2.6
sysname: S-(2-hydroxyacyl)glutathione hydrolase
comment: Also hydrolyses S-acetoacetylglutathione, but more slowly.
reaction: S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate [RN:R04090]
iubmb_reaction: R04090 > R01736
name:
--- 
- hydroxyacylglutathione hydrolase
- glyoxalase II
- S-2-hydroxylacylglutathione hydrolase
- acetoacetylglutathione hydrolase


entry: 3.1.2.8
name: --- - Deleted entry
comment:
Deleted entry: S-acetoacylglutathione hydrolase. Now included with EC 3.1.2.6 hydroxyacylglutathione hydrolase (EC 3.1.2.8 created 1961, deleted 1978)


entry: 3.1.2.11
sysname: acetoacetyl-CoA hydrolase
reaction: acetoacetyl-CoA + H2O = CoA + acetoacetate [RN:R01358]
iubmb_reaction: R01358
name:
--- 
- acetoacetyl-CoA hydrolase
- acetoacetyl coenzyme A hydrolase
- acetoacetyl CoA deacylase
- acetoacetyl coenzyme A deacylase


entry: 3.1.2.14
sysname: oleoyl-[acyl-carrier-protein] hydrolase
reaction: oleoyl-[acyl-carrier protein] + H2O = [acyl-carrier protein] + oleate [RN:R02814]
iubmb_reaction: R02814
kegg_reaction: R01706
name:
--- 
- oleoyl-[acyl-carrier-protein] hydrolase
- acyl-[acyl-carrier-protein] hydrolase
- acyl-ACP-hydrolase
- acyl-acyl carrier protein hydrolase
- oleoyl-ACP thioesterase
- oleoyl-acyl carrier protein thioesterase

comment:
Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.


entry: 3.1.2.15
sysname: ubiquitin-C-terminal-thioester hydrolase
reaction: ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol [RN:R02418]
iubmb_reaction: R02418
name:
--- 
- ubiquitin thiolesterase
- ubiquitin carboxy-terminal esterase
- isopeptidase
- isopeptidase T
- ubiquitin C-terminal hydrolase
- ubiquitin carboxy-terminal hydrolase
- ubiquitin-C-terminal-thiolester hydrolase

comment:
Acts on esters formed between thiols such as dithiothreitol or glutathione and the C-terminal glycine residue of the polypeptide ubiquitin. Also acts on AMP-ubiquitin. May be the same as EC 3.4.19.12, ubiquitinyl hydrolase 1.


entry: 3.1.2.16
name: --- - citrate lyase deacetylase - "[citrate-(pro-3S)-lyase] thiolesterase"
sysname: [citrate-(pro-3S)-lyase](acetyl-form) hydrolase
comment: Hydrolysis inactivates EC 4.1.3.6 citrate (pro-3S)-lyase.
iubmb_reaction: R04450
reaction:
[citrate (pro-3S)-lyase](acetyl form) + H2O = [citrate (pro-3S)-lyase](thiol form) + acetate [RN:R04450]


entry: 3.1.2.18
sysname: ADP-dependent-short-chain-acyl-CoA hydrolase
comment: Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA.
reaction: acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
iubmb_reaction: R00383
name:
--- 
- ADP-dependent short-chain-acyl-CoA hydrolase
- short-chain acyl coenzyme A hydrolase
- propionyl coenzyme A hydrolase
- propionyl-CoA hydrolase
- propionyl-CoA thioesterase
- short-chain acyl-CoA hydrolase
- short-chain acyl-CoA thioesterase


entry: 3.1.2.19
sysname: ADP-dependent-medium-chain-acyl-CoA hydrolase
comment: Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA.
reaction: acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
iubmb_reaction: R00383
name:
--- 
- ADP-dependent medium-chain-acyl-CoA hydrolase
- medium-chain acyl coenzyme A hydrolase
- medium-chain acyl-CoA hydrolase
- medium-chain acyl-thioester hydrolase
- medium-chain hydrolase
- myristoyl-CoA thioesterase


entry: 3.1.2.20
sysname: acyl-CoA hydrolase
reaction: acyl-CoA + H2O = CoA + a carboxylate [RN:R00383]
iubmb_reaction: R00383
name:
--- 
- acyl-CoA hydrolase
- acyl coenzyme A thioesterase
- acyl-CoA thioesterase
- acyl coenzyme A hydrolase
- thioesterase B
- thioesterase II

comment:
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)


entry: 3.1.2.21
sysname: dodecanoyl-[acyl-carrier-protein] hydrolase
reaction: dodecanoyl-[acyl-carrier protein] + H2O = [acyl-carrier protein] + dodecanoate [RN:R04014]
iubmb_reaction: R04014
name:
--- 
- dodecanoyl-[acyl-carrier protein] hydrolase
- lauryl-acyl-carrier-protein hydrolase
- dodecanoyl-acyl-carrier-protein hydrolase
- dodecyl-acyl-carrier protein hydrolase

comment:
acts on the acyl-carrier-protein thioester of C12 and, with a much lower activity, C14 fatty acids. The derivative of oleic acid is hydrolysed very slowly (cf. EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase).


entry: 3.1.2.22
sysname: palmitoyl[protein] hydrolase
reaction: palmitoyl[protein] + H2O = palmitate + protein [RN:R01705]
iubmb_reaction: R01705
kegg_reaction: R01274
name:
--- 
- palmitoyl[protein] hydrolase
- palmitoyl-protein thioesterase
- palmitoyl-(protein) hydrolase

comment:
specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.


entry: 3.1.2.24
name: --- - Transferred to 3.13.1.3
comment:
Transferred entry: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase, the enzyme was incorrectly classified as a thioester hydrolase when the bond broken is a C-S bond, which is not an ester. Now EC 3.13.1.3, 2'-hydroxybiphenyl-2-sulfinate desulfinase (EC 3.1.2.24 created 2000, deleted 2005)


entry: 3.1.2.25
name: --- - phenylacetyl-CoA hydrolase
sysname: phenylglyoxylyl-CoA hydrolase
reaction: phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA [RN:R07294]
iubmb_reaction: R07294
comment:
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.


entry: 3.1.2.26
name: --- - bile-acid-CoA hydrolase
sysname: deoxycholoyl-CoA hydrolase
reaction: deoxycholoyl-CoA + H2O = CoA + deoxycholate [RN:R07295]
iubmb_reaction: R07295
comment:
Choloyl-CoA, 3-dehydrocholoyl-CoA and chenodeoxycholoyl-CoA can also act as substrates, but acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA and phenylacetyl-CoA cannot.


entry: 3.1.2.27
sysname: choloyl-CoA hydrolase
reaction: choloyl-CoA + H2O = cholate + CoA [RN:R07296]
iubmb_reaction: R07296
name:
--- 
- choloyl-CoA hydrolase
- PTE-2 (ambiguous)
- choloyl-coenzyme A thioesterase
- chenodeoxycholoyl-coenzyme A thioesterase
- peroxisomal acyl-CoA thioesterase 2

comment:
Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoAs, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoAs, all of which are present in peroxisomes. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome [1].


entry: 3.1.2.-
name: --- []
reaction:
(1) 2-Ketocyclohexane-1-carboxyl-CoA + H2O <=> 6-Carboxyhexanoyl-CoA [RN:R05592]; (2) 6-Oxo-2-hydroxycyclohexane-1-carboxyl-CoA + H2O <=> 3-Hydroxypimeloyl-CoA [RN:R05593]; (3) 3-Isopropylbut-3-enoyl-CoA + H2O <=> 3-Isopropylbut-3-enoic acid + CoA [RN:R06415]; (4) 1,4-Dihydroxy-2-naphthoyl-CoA + H2O <=> 1,4-Dihydroxy-2-naphthoate + CoA [RN:R07262]


entry: 3.1.3.1
sysname: phosphate-monoester phosphohydrolase (alkaline optimum)
reaction: A phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
iubmb_reaction: R00626 > R01010 R03024
kegg_reaction: R04620
name:
--- 
- alkaline phosphatase
- alkaline phosphomonoesterase
- phosphomonoesterase
- glycerophosphatase
- alkaline phosphohydrolase
- alkaline phenyl phosphatase
- orthophosphoric-monoester phosphohydrolase (alkaline optimum)

comment:
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)


entry: 3.1.3.2
sysname: phosphate-monoester phosphohydrolase (acid optimum)
comment: Wide specificity. Also catalyses transphosphorylations.
reaction: A phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
iubmb_reaction: R00626 > R00548 R03024
name:
--- 
- acid phosphatase
- acid phosphomonoesterase
- phosphomonoesterase
- glycerophosphatase
- acid monophosphatase
- acid phosphohydrolase
- acid phosphomonoester hydrolase
- uteroferrin
- acid nucleoside diphosphate phosphatase
- orthophosphoric-monoester phosphohydrolase (acid optimum)


entry: 3.1.3.4
sysname: 3-sn-phosphatidate phosphohydrolase
reaction: A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
iubmb_reaction: R02239
kegg_reaction: R04162 R06520 R06521 R06522
name:
--- 
- phosphatidate phosphatase
- phosphatic acid phosphatase
- acid phosphatidyl phosphatase
- phosphatic acid phosphohydrolase


entry: 3.1.3.5
sysname: 5'-ribonucleotide phosphohydrolase
comment: Wide specificity for 5'-nucleotides.
reaction: A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
iubmb_reaction: R07297 > R00183 R00511 R00963 R01126 R01227 R02323 R02719 R03346
kegg_reaction: R01569 R01664 R01968 R02088
name:
--- 
- 5'-nucleotidase
- uridine 5'-nucleotidase
- 5'-adenylic phosphatase
- adenosine 5'-phosphatase
- AMP phosphatase
- adenosine monophosphatase
- 5'-mononucleotidase
- AMPase
- UMPase
- snake venom 5'-nucleotidase
- thimidine monophosphate nucleotidase
- 5'-AMPase
- 5'-AMP nucleotidase
- AMP phosphohydrolase
- IMP 5'-nucleotidase


entry: 3.1.3.7
sysname: adenosine-3'(2'),5'-bisphosphate 3'(2')-phosphohydrolase
comment: Also acts on 3'-phosphoadenylyl sulfate, and on the corresponding 2'-phosphates.
reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate [RN:R00188]
iubmb_reaction: R00188
kegg_reaction: R00508
name:
--- 
- 3'(2'),5'-bisphosphate nucleotidase
- phosphoadenylate 3'-nucleotidase
- 3'-phosphoadenylylsulfate 3'-phosphatase
- 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase


entry: 3.1.3.8
name: --- - 3-phytase - 1-phytase - phytase - phytate 1-phosphatase - phytate 6-phosphatase
sysname: myo-inositol-hexakisphosphate 3-phosphohydrolase
iubmb_reaction: R03371
reaction:
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate [RN:R03371]


entry: 3.1.3.9
name: --- - glucose-6-phosphatase - glucose 6-phosphate phosphatase
sysname: D-glucose-6-phosphate phosphohydrolase
reaction: D-glucose 6-phosphate + H2O = D-glucose + phosphate [RN:R00303]
iubmb_reaction: R00303 > R01788
comment:
Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate-hexose phosphotransferase), EC 2.7.1.79 (diphosphate-glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].


entry: 3.1.3.11
sysname: D-fructose-1,6-bisphosphate 1-phosphohydrolase
comment: The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00762]
iubmb_reaction: R00762 > R04780
kegg_reaction: R01845
name:
--- 
- fructose-bisphosphatase
- hexose diphosphatase
- FBPase
- fructose 1,6-diphosphatase
- fructose 1,6-diphosphate phosphatase
- D-fructose 1,6-diphosphatase
- fructose 1,6-bisphosphatase
- fructose diphosphatase
- fructose diphosphate phosphatase
- fructose bisphosphate phosphatase
- fructose 1,6-bisphosphate 1-phosphatase
- fructose 1,6-bisphosphate phosphatase
- hexose bisphosphatase
- D-fructose-1,6-bisphosphate phosphatase


entry: 3.1.3.13
sysname: 2,3-bisphospho-D-glycerate 2-phosphohydrolase
reaction: 2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate [RN:R01516]
iubmb_reaction: R01516
name:
--- 
- bisphosphoglycerate phosphatase
- 2,3-diphosphoglycerate phosphatase
- diphosphoglycerate phosphatase
- 2,3-diphosphoglyceric acid phosphatase
- 2,3-bisphosphoglycerate phosphatase
- glycerate-2,3-diphosphate phosphatase


entry: 3.1.3.15
sysname: L-histidinol-phosphate phosphohydrolase
reaction: L-histidinol phosphate + H2O = L-histidinol + phosphate [RN:R03013]
iubmb_reaction: R03013
name:
--- 
- histidinol-phosphatase
- histidinol phosphate phosphatase
- L-histidinol phosphate phosphatase
- histidinolphosphate phosphatase
- HPpase
- histidinolphosphatase


entry: 3.1.3.16
sysname: phosphoprotein phosphohydrolase
reaction: A phosphoprotein + H2O = a protein + phosphate [RN:R00164]
iubmb_reaction: R00164
name:
--- 
- phosphoprotein phosphatase
- protein phosphatase-1
- protein phosphatase-2A
- protein phosphatase-2B
- protein phosphatase-2C
- protein D phosphatase
- phosphospectrin phosphatase
- casein phosphatase
- Aspergillus awamori acid protein phosphatase
- calcineurin
- phosphatase 2A
- phosphatase 2B
- phosphatase II
- phosphatase IB
- phosphatase C-II
- polycation modulated (PCM-) phosphatase
- phosphopyruvate dehydrogenase phosphatase
- phosphatase SP
- branched-chain alpha-keto acid dehydrogenase phosphatase
- BCKDH phosphatase
- 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase
- HMG-CoA reductase phosphatase
- phosphatase H-II
- phosphatase III
- phosphatase I
- protein phosphatase
- phosphatase IV

comment:
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1 phosphoamidase)


entry: 3.1.3.17
sysname: [phosphorylase a] phosphohydrolase
reaction: [phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate [RN:R00077]
iubmb_reaction: R00077
name:
--- 
- "[phosphorylase] phosphatase"
- PR-enzyme
- phosphorylase a phosphatase
- glycogen phosphorylase phosphatase
- protein phosphatase C
- type 1 protein phosphatase


entry: 3.1.3.18
sysname: 2-phosphoglycolate phosphohydrolase
reaction: 2-phosphoglycolate + H2O = glycolate + phosphate [RN:R01334]
iubmb_reaction: R01334
name:
--- 
- phosphoglycolate phosphatase
- phosphoglycolate hydrolase
- 2-phosphoglycolate phosphatase
- P-glycolate phosphatase
- phosphoglycollate phosphatase


entry: 3.1.3.19
sysname: glycerol-2-phosphate phosphohydrolase
reaction: glycerol 2-phosphate + H2O = glycerol + phosphate [RN:R01043]
iubmb_reaction: R01043
name:
--- 
- glycerol-2-phosphatase
- beta-glycerophosphatase
- beta-glycerophosphate phosphatase
- 2-glycerophosphatase


entry: 3.1.3.20
sysname: D-glycerate-2-phosphate phosphohydrolase
reaction: D-glycerate 2-phosphate + H2O = D-glycerate + phosphate [RN:R01748]
iubmb_reaction: R01748
name:
--- 
- phosphoglycerate phosphatase
- D-2-phosphoglycerate phosphatase
- glycerophosphate phosphatase


entry: 3.1.3.21
sysname: glycerol-1-phosphate phosphohydrolase
reaction: glycerol 1-phosphate + H2O = glycerol + phosphate [RN:R07298]
iubmb_reaction: R07298
kegg_reaction: R00841
name:
--- 
- glycerol-1-phosphatase
- alpha-glycerophosphatase
- alpha-glycerol phosphatase
- glycerol 3-phosphatase
- glycerol-3-phosphate phosphatase
- glycerol 3-phosphate phosphohydrolase

comment:
The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate. The enzyme from yeast also acts on propane-1,2-diol 1-phosphate, but not on a variety of other phosphate esters.


entry: 3.1.3.23
name: --- - sugar-phosphatase
sysname: sugar-phosphate phosphohydrolase
reaction: sugar phosphate + H2O = sugar + phosphate [RN:R00804]
iubmb_reaction: R00804
comment:
Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate.


entry: 3.1.3.24
sysname: sucrose-6F-phosphate phosphohydrolase
reaction: sucrose 6F-phosphate + H2O = sucrose + phosphate [RN:R00805 R06211]
iubmb_reaction: R00805 R06211(G)
name:
--- 
- sucrose-phosphatase
- sucrose 6-phosphate hydrolase
- sucrose-phosphate hydrolase
- sucrose-phosphate phosphohydrolase
- sucrose-6-phosphatase


entry: 3.1.3.25
sysname: myo-inositol-phosphate phosphohydrolase
reaction: myo-inositol phosphate + H2O = myo-inositol + phosphate [RN:R07343]
iubmb_reaction: R07343 > R01185 R01186 R01187
name:
--- 
- inositol-phosphate phosphatase
- myo-inositol-1(or 4)-monophosphatase
- inositol 1-phosphatase
- L-myo-inositol-1-phosphate phosphatase
- myo-inositol 1-phosphatase
- inositol phosphatase
- inositol monophosphate phosphatase
- inositol-1(or 4)-monophosphatase
- myo-inositol-1(or 4)-phosphate phosphohydrolase
- myo-inositol monophosphatase
- myo-inositol-1-phosphatase

comment:
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known [4].


entry: 3.1.3.26
sysname: myo-inositol-hexakisphosphate 6-phosphohydrolase
iubmb_reaction: R03372
name:
--- 
- 4-phytase
- 6-phytase (name based on 1L-numbering system and not 1D-numbering)
- phytase
- phytate 6-phosphatase

reaction:
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate [RN:R03372]


entry: 3.1.3.27
sysname: phosphatidylglycerophosphate phosphohydrolase
reaction: phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate [RN:R02029]
iubmb_reaction: R02029
name:
--- 
- phosphatidylglycerophosphatase
- phosphatidylglycerol phosphate phosphatase
- phosphatidylglycerol phosphatase
- PGP phosphatase


entry: 3.1.3.29
sysname: N-acylneuraminate-9-phosphate phosphohydrolase
reaction: N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate [RN:R02597]
iubmb_reaction: R02597 > R01805
name:
--- 
- N-acylneuraminate-9-phosphatase
- acylneuraminate 9-phosphatase
- N-acylneuraminic acid 9-phosphate phosphatase
- N-acylneuraminic (sialic) acid 9-phosphatase


entry: 3.1.3.30
name: --- - Deleted entry
comment:
Deleted entry: 3'-phosphoadenylylsulfate 3'-phosphatase. Now included with EC 3.1.3.7 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.30 created 1972, deleted 1992)


entry: 3.1.3.31
sysname: nucleotide phosphohydrolase
reaction: A nucleotide + H2O = a nucleoside + phosphate [RN:R01572]
iubmb_reaction: R01572
name:
--- 
- nucleotidase
- nucleotide phosphatase
- nucleotide-specific phosphatase
- NSP I
- NSP II
- deoxyribonucleoside-activated nucleotidase (DAN)
- deoxyinosine-activated nucleotidase (DIAN)
- acid nucleotidase

comment:
A wide specificity for 2', 3'- and 5'- nucleotides; also hydrolyses glycerol phosphate and 4-nitrophenyl phosphate.


entry: 3.1.3.32
sysname: polynucleotide 3'-phosphohydrolase
reaction: A 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate [RN:R02248]
iubmb_reaction: R02248
name:
--- 
- polynucleotide 3'-phosphatase
- 2'(3')-polynucleotidase
- DNA 3'-phosphatase
- deoxyribonucleate 3'-phosphatase
- 5'-polynucleotidekinase 3'-phosphatase

comment:
Also hydrolyses nucleoside 2'-, 3'- and 5'-monophosphates, but only 2'- and 3'-phosphopolynucleotides.


entry: 3.1.3.34
name: --- - deoxynucleotide 3'-phosphatase - 3'-deoxynucleotidase - 3'-deoxyribonucleotidase
sysname: deoxyribonucleotide 3'-phosphohydrolase
reaction: A deoxynucleoside 3'-phosphate + H2O = a deoxynucleoside + phosphate [RN:R02751]
iubmb_reaction: R02751
comment:
Also catalyses the selective removal of 3'-phosphate groups from DNA and oligodeoxynucleotides. Induced in Escherichia coli by T-even phages.


entry: 3.1.3.35
sysname: thymidylate 5'-phosphohydrolase
comment: Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP.
reaction: thymidylate + H2O = thymidine + phosphate [RN:R01569]
iubmb_reaction: R01569
name:
--- 
- thymidylate 5'-phosphatase
- thymidylate 5'-nucleotidase
- deoxythymidylate 5'-nucleotidase
- thymidylate nucleotidase
- deoxythymidylic 5'-nucleotidase
- deoxythymidylate phosphohydrolase
- dTMPase


entry: 3.1.3.36
sysname: phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase
iubmb_reaction: R04404
name:
--- 
- phosphoinositide 5-phosphatase
- type II inositol polyphosphate 5-phosphatase
- triphosphoinositide phosphatase
- IP3 phosphatase
- PtdIns(4,5)P2 phosphatase
- triphosphoinositide phosphomonoesterase
- diphosphoinositide phosphatase
- inositol 1,4,5-triphosphate 5-phosphomonoesterase
- inositol triphosphate 5-phosphomonoesterase
- phosphatidylinositol-bisphosphatase
- phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase
- phosphatidylinositol 4,5-bisphosphate phosphatase
- polyphosphoinositol lipid 5-phosphatase
- phosphatidyl-inositol-bisphosphate phosphatase

comment:
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.

reaction:
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate [RN:R04404]


entry: 3.1.3.37
sysname: sedoheptulose-1,7-bisphosphate 1-phosphohydrolase
reaction: sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate [RN:R01845]
iubmb_reaction: R01845
name:
--- 
- sedoheptulose-bisphosphatase
- SBPase
- sedoheptulose 1,7-diphospate phosphatase
- sedoheptulose 1,7-diphosphatase
- sedoheptulose diphosphatase
- sedoheptulose bisphosphatase
- sedoheptulose 1,7-bisphosphatase


entry: 3.1.3.39
sysname: streptomycin-6-phosphate phosphohydrolase
comment: Also acts on dihydrostreptomycin 3'alpha,6-bisphosphate and streptidine 6-phosphate.
reaction: streptomycin 6-phosphate + H2O = streptomycin + phosphate [RN:R02228]
iubmb_reaction: R02228
name:
--- 
- streptomycin-6-phosphatase
- streptomycin 6-phosphate phosphatase
- streptomycin 6-phosphate phosphohydrolase
- streptomycin-6-P phosphohydrolase


entry: 3.1.3.40
sysname: 1-guanidino-1-deoxy-scyllo-inositol-4-phosphate 4-phosphohydrolase
iubmb_reaction: R03496
name:
--- 
- guanidinodeoxy-scyllo-inositol-4-phosphatase
- 1-guanidino-scyllo-inositol 4-phosphatase
- 1-guanidino-1-deoxy-scyllo-inositol-4-P phosphohydrolase

reaction:
1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H2O = 1-guanidino-1-deoxy-scyllo-inositol + phosphate [RN:R03496]


entry: 3.1.3.41
sysname: 4-nitrophenylphosphate phosphohydrolase
reaction: 4-nitrophenyl phosphate + H2O = 4-nitrophenol + phosphate [RN:R03024]
iubmb_reaction: R03024
name:
--- 
- 4-nitrophenylphosphatase
- nitrophenyl phosphatase
- p-nitrophenylphosphatase
- para-nitrophenyl phosphatase
- K-pNPPase
- NPPase
- PNPPase
- Ecto-p-nitrophenyl phosphatase
- p-nitrophenylphosphate phosphohydrolase

comment:
A number of other substances, including phenyl phosphate, 4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are not substrates.


entry: 3.1.3.42
sysname: [UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D] phosphohydrolase
comment: The product is EC 2.4.1.11 glycogen(starch) synthase.
reaction: [glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate [RN:R04156]
iubmb_reaction: R04156
name:
--- 
- "[glycogen-synthase-D] phosphatase"
- uridine diphosphoglucose-glycogen glucosyltransferase phosphatase
- UDP-glycogen glucosyltransferase phosphatase
- UDPglucose-glycogen glucosyltransferase phosphatase
- glycogen glucosyltransferase phosphatase
- glycogen synthetase phosphatase
- glycogen synthase phosphatase
- glycogen synthase D phosphatase
- Mg2+ dependent glycogen synthase phosphatase
- phosphatase type 2degC


entry: 3.1.3.43
sysname: [pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase
iubmb_reaction: R03450
name:
--- 
- "[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase"
- pyruvate dehydrogenase phosphatase
- phosphopyruvate dehydrogenase phosphatase
- "[pyruvate dehydrogenase (lipoamide)]-phosphatase"
- "[pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase"

comment:
A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex.

reaction:
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate [RN:R03450]


entry: 3.1.3.44
name: --- - "[acetyl-CoA carboxylase]-phosphatase"
sysname: [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase
reaction: [acetyl-CoA carboxylase] phosphate + H2O = [acetyl-CoA carboxylase] + phosphate [RN:R03273]
iubmb_reaction: R03273
comment:
Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA carboxylase. Acts similarly on EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase), EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC 3.1.3.17 ([phosphorylase] phosphatase) or EC 3.1.3.43 {[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase}.


entry: 3.1.3.45
name: --- - 3-deoxy-manno-octulosonate-8-phosphatase
sysname: 3-deoxy-D-manno-octulosonate-8-phosphate 8-phosphohydrolase
iubmb_reaction: R03350
reaction:
3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate [RN:R03350]


entry: 3.1.3.46
sysname: beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
reaction: beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00763]
iubmb_reaction: R00763 > R02731
name:
--- 
- fructose-2,6-bisphosphate 2-phosphatase
- fructose-2,6-bisphosphatase
- D-fructose-2,6-bisphosphate 2-phosphohydrolase

comment:
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).


entry: 3.1.3.47
name: --- - "[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase" - reductase phosphatase
sysname: [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate phosphohydrolase
iubmb_reaction: R04542
comment:
Acts on the product of the reaction catalysed by EC 2.7.1.109 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, simultaneously dephosphorylating and activating EC 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH).

reaction:
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O = [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate [RN:R04542]


entry: 3.1.3.48
sysname: protein-tyrosine-phosphate phosphohydrolase
reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate [RN:R02585]
iubmb_reaction: R02585
name:
--- 
- protein-tyrosine-phosphatase
- phosphotyrosine phosphatase
- phosphoprotein phosphatase (phosphotyrosine)
- phosphotyrosine histone phosphatase
- protein phosphotyrosine phosphatase
- tyrosylprotein phosphatase
- phosphotyrosine protein phosphatase
- phosphotyrosylprotein phosphatase
- tyrosine O-phosphate phosphatase
- PPT-phosphatase
- PTPase
- "[phosphotyrosine]protein phosphatase"
- PTP-phosphatase

comment:
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.1.112 protein-tyrosine kinase.


entry: 3.1.3.49
name: --- - "[pyruvate kinase]-phosphatase" - pyruvate kinase phosphatase
sysname: [ATP:pyruvate 2-O-phosphotransferase]-phosphate phosphohydrolase
reaction: [pyruvate kinase] phosphate + H2O = [pyruvate kinase] + phosphate [RN:R03993]
iubmb_reaction: R03993
comment:
Simultaneously dephosphorylates and activates EC 2.7.1.40 pyruvate kinase, that has been inactivated by protein kinase.


entry: 3.1.3.51
sysname: dolichyl-phosphate phosphohydrolase
reaction: dolichyl phosphate + H2O = dolichol + phosphate [RN:R01003]
iubmb_reaction: R01003
name:
--- 
- dolichyl-phosphatase
- dolichol phosphate phosphatase
- dolichol phosphatase
- dolichol monophosphatase
- dolichyl monophosphate phosphatase
- dolichyl phosphate phosphatase
- polyisoprenyl phosphate phosphatase
- polyprenylphosphate phosphatase
- Dol-P phosphatase


entry: 3.1.3.52
sysname: [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphate phosphohydrolase
iubmb_reaction: (other) R03515
kegg_reaction: R03515
name:
--- 
- "[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase"
- branched-chain oxo-acid dehydrogenase phosphatase
- branched-chain 2-keto acid dehydrogenase phosphatase
- branched-chain alpha-keto acid dehydrogenase phosphatase
- BCKDH
- "[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase"
- "[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphate phosphohydrolase"

comment:
A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. Simultaneously dephosphorylates and activates EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), that has been inactivated by phosphorylation.

reaction:
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H2O = [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate


entry: 3.1.3.53
sysname: [myosin-light-chain]-phosphate phosphohydrolase
reaction: [myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate [RN:R03151]
iubmb_reaction: R03151
name:
--- 
- "[myosin-light-chain] phosphatase"
- myosin light chain kinase phosphatase
- myosin phosphatase
- protein phosphatase 2A
- myosin-light-chain-phosphatase

comment:
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.1.117, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.


entry: 3.1.3.54
sysname: beta-D-fructose-2,6-bisphosphate 6-phosphohydrolase
comment: cf. EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
reaction: beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructofuranose 2-phosphate + phosphate [RN:R02730]
iubmb_reaction: R02730
name:
--- 
- fructose-2,6-bisphosphate 6-phosphatase
- fructose 2,6-bisphosphate-6-phosphohydrolase
- fructose-2,6-bisphosphate 6-phosphohydrolase
- D-fructose-2,6-bisphosphate 6-phosphohydrolase


entry: 3.1.3.56
sysname: 1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
iubmb_reaction: R03394 R03430
name:
--- 
- inositol-polyphosphate 5-phosphatase
- type I inositol-polyphosphate phosphatase
- inositol trisphosphate phosphomonoesterase
- InsP3/Ins(1,3,4,5)P4 5-phosphatase
- inosine triphosphatase
- D-myo-inositol 1,4,5-triphosphate 5-phosphatase
- D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
- L-myo-inositol 1,4,5-trisphosphate-monoesterase
- inositol phosphate 5-phosphomonoesterase
- inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase
- Ins(1,4,5)P3 5-phosphatase
- D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase
- inositol 1,4,5-trisphosphate phosphatase
- inositol polyphosphate-5-phosphatase
- myo-inositol-1,4,5-trisphosphate 5-phosphatase
- inositol-1,4,5-trisphosphate 5-phosphatase

comment:
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.

reaction:
(1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]; (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]


entry: 3.1.3.57
name: --- - inositol-1,4-bisphosphate 1-phosphatase - inositol-polyphosphate 1-phosphatase
sysname: 1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase
reaction: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate [RN:R03393]
iubmb_reaction: R03393
kegg_reaction: R03427
comment:
The enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar V(max) values for both substrates, but with a five-times higher affinity for the bisphosphate. Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.


entry: 3.1.3.58
name: --- - sugar-terminal-phosphatase - xylitol-5-phosphatase
sysname: sugar-omega-phosphate phosphohydrolase
reaction: D-glucose 6-phosphate + H2O = D-glucose + phosphate [RN:R00303]
iubmb_reaction: R00303
comment:
Acts on sugars and polyols phosphorylated on the terminal carbon, with a preference for sugars with a D-erythro-configuration, e.g. good substrates are glucose 6-phosphate, mannose 6-phosphate, 6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate.


entry: 3.1.3.59
sysname: 1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase
comment: Involved in the biosynthesis of thrombocyte activating factor in animal tissues.
iubmb_reaction: R03454
name:
--- 
- alkylacetylglycerophosphatase
- 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase
- alkylacetylglycerophosphate phosphatase

reaction:
1-alkyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-alkyl-2-acetyl-sn-glycerol + phosphate [RN:R03454]


entry: 3.1.3.61
name: --- - Deleted entry
comment:
Deleted entry: inositol-1,4,5-trisphosphate 1-phosphatase, as its existence has not been established (EC 3.1.3.61 created 1992, deleted 2002)


entry: 3.1.3.62
sysname: 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase
comment: This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3.
reaction: myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate
iubmb_reaction: (other) R03434
kegg_reaction: R03434
name:
--- 
- multiple inositol-polyphosphate phosphatase
- inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
- inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase
- inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase
- inositol tetrakisphosphate phosphomonoesterase
- inositol-1,3,4,5-tetrakisphosphate 3-phosphatase
- MIPP


entry: 3.1.3.63
sysname: 2-carboxy-D-arabinitol-1-phosphate 1-phosphohydrolase
reaction: 2-carboxy-D-arabinitol 1-phosphate + H2O = 2-carboxy-D-arabinitol + phosphate [RN:R04167]
iubmb_reaction: R04167
name:
--- 
- 2-carboxy-D-arabinitol-1-phosphatase
- 2-carboxyarabinitol 1-phosphatase
- 2-carboxy-D-arabinitol 1-phosphate phosphohydrolase


entry: 3.1.3.64
sysname: 1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase
iubmb_reaction: R03363
kegg_reaction: R03330 R06875
name:
--- 
- phosphatidylinositol-3-phosphatase
- inositol-1,3-bisphosphate 3-phosphatase
- inositol 1,3-bisphosphate phosphatase
- inositol-polyphosphate 3-phosphatase
- D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase
- phosphatidyl-3-phosphate 3-phosphohydrolase

comment:
This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3)P2 to Ins-1-P.

reaction:
1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate [RN:R03363]


entry: 3.1.3.65
name: --- - Deleted entry
comment:
Deleted entry: inositol-1,3-bisphosphate 3-phosphatase. Now included with EC 3.1.3.64, phosphatidylinositol-3-phosphatase(EC 3.1.3.65 created 1992, deleted 2002)


entry: 3.1.3.66
sysname: 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase
iubmb_reaction: R07299
kegg_reaction: R04372
name:
--- 
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- inositol-3,4-bisphosphate 4-phosphatase
- D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase
- phosphoinositide 4-phosphatase
- inositol polyphosphate 4-phosphatase
- inositol polyphosphate 4-phosphatase type II

comment:
Mg2+-independent. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4)P3 to Ins(1,3)P2. It also converts Ins(3,4)P2 into Ins-3-P.

reaction:
1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]


entry: 3.1.3.67
sysname: 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase
iubmb_reaction: R04513
name:
--- 
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- PTEN, MMAC1
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase

comment:
Requires Mg2+. Does not dephosphorylate inositol 4,5-bisphosphate. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4,5)P4 to Ins(1,4,5)P3

reaction:
phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate [RN:R04513]


entry: 3.1.3.69
name: --- - glucosylglycerol 3-phosphatase - salt tolerance protein A, StpA
sysname: 2-(beta-D-glucosyl)-sn-glycerol-3-phosphate phosphohydrolase
iubmb_reaction: R05791
comment:
Acts with EC 2.4.1.213 (glucosylglycerol-phosphate synthase) to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.

reaction:
2-(beta-D-glucosyl)-sn-glycerol-3-phosphate + H2O = 2-(beta-D-glucosyl)-sn-glycerol + phosphate [RN:R05791]


entry: 3.1.3.70
name: --- - mannosyl-3-phosphoglycerate phosphatase
sysname: alpha-D-mannosyl-3-phosphoglycerate phosphohydrolase
iubmb_reaction: R05790
comment:
Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.

reaction:
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2(alpha-D-mannosyl)-D-glycerate + phosphate [RN:R05790]


entry: 3.1.3.71
sysname: (R)-2-phospho-3-sulfolactate phosphohydrolase
reaction: (2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate [RN:R05789]
iubmb_reaction: R05789
name:
--- 
- 2-phosphosulfolactate phosphatase
- (2R)-phosphosulfolactate phosphohydrolase
- ComB phosphatase

comment:
Requires Mg2+. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyses a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This enzyme can also hydrolyze phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.


entry: 3.1.3.73
name: --- - alpha-ribazole phosphatase - CobC
sysname: alpha-ribazole-5'-phosphate phosphohydrolase
reaction: alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate [RN:R04594]
iubmb_reaction: R04594
comment:
In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU. CobS catalyses the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with alpha-ribazole to yield adenosylcobalamin.


entry: 3.1.3.74
sysname: pyridoxal-5'-phosphate phosphohydrolase
reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate [RN:R00173]
iubmb_reaction: R00173
kegg_reaction: R01911 R02494
name:
--- 
- pyridoxal phosphatase
- vitamine B6 (pyridoxine) phosphatase
- PLP phosphatase
- vitamin B6-phosphate phosphatase
- PNP phosphatase

comment:
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.


entry: 3.1.3.75
name: --- - phosphoethanolamine/phosphocholine phosphatase - PHOSPHO1 - 3X11A
sysname: phosphoethanolamine phosphohydrolase
iubmb_reaction: R06870 R06871
comment:
Requires active site Mg2+ but also works, to a lesser extent, with Co2+ and Mn2+. The enzyme is highly specific for phosphoethanolamine and phosphocholine.

reaction:
(1) O-phosphoethanolamine + H2O = ethanolamine + phosphate [RN:R06870]; (2) phosphocholine + H2O = choline + phosphate [RN:R06871]


entry: 3.1.3.76
sysname: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase
name:
--- 
- lipid-phosphate phosphatase
- hydroxy fatty acid phosphatase
- dihydroxy fatty acid phosphatase
- hydroxy lipid phosphatase
- sEH (ambiguous)
- soluble epoxide hydrolase (ambiguous)

comment:
Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1]. The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form [1]. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals [1].

reaction:
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate


entry: 3.1.3.77
name: --- - acireductone synthase - E1 - E-1 enolase-phosphatase
sysname: 5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing)
iubmb_reaction: (other) R07393 R07394 R07395
kegg_reaction: R07393 R07394 R07395
comment:
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [2]. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylthio)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-methylthio-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].

reaction:
(1) 5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate; (2) (1a) 5-(methylthio)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate; (3) (1b) 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate


entry: 3.1.3.-
name: --- []
reaction:
(1) NADP+ + H2O <=> Orthophosphate + NAD+ [RN:R00118]; (2) beta-D-Fructose 2-phosphate + H2O <=> D-Fructose + Orthophosphate [RN:R00872]; (3) Thiamin + Orthophosphate <=> Thiamin monophosphate + H2O [RN:R02135]; (4) N-Acetyl-D-mannosamine + Orthophosphate <=> N-Acetyl-D-mannosamine 6-phosphate + H2O [RN:R02706]; (5) Sphinganine 1-phosphate + H2O <=> Sphinganine + Orthophosphate [RN:R06520]; (6) Sphingosine 1-phosphate + H2O <=> Sphingosine + Orthophosphate [RN:R06521]; (7) Ceramide 1-phosphate + H2O <=> N-Acylsphingosine + Orthophosphate [RN:R06522]; (8) 5-Amino-6-(5'-phosphoribitylamino)uracil + H2O <=> 4-(1-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine + Orthophosphate [RN:R07280]; (9) 2-Acyl-1-(1-alkenyl)-sn-glycero-3-phosphate + H2O <=> 1-Alkenyl-2-acylglycerol + Orthophosphate [RN:R07383]


entry: 3.1.4.1
sysname: oligonucleate 5'-nucleotidohydrolase
comment: Low activity towards polynucleotides. A 3'-phosphate terminus on the substrate inhibits hydrolysis.
name:
--- 
- phosphodiesterase I
- 5'-exonuclease
- 5'-phosphodiesterase
- 5'-nucleotide phosphodiesterase

reaction:
Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides


entry: 3.1.4.2
sysname: sn-glycero-3-phosphocholine glycerophosphohydrolase
comment: Also acts on sn-glycero-3-phosphoethanolamine.
reaction: sn-glycero-3-phosphocholine + H2O = choline + sn-glycerol 3-phosphate [RN:R01030]
iubmb_reaction: R01030
kegg_reaction: R01470
name:
--- 
- glycerophosphocholine phosphodiesterase
- glycerophosphinicocholine diesterase
- glycerylphosphorylcholinediesterase
- sn-glycero-3-phosphorylcholine diesterase
- glycerolphosphorylcholine phosphodiesterase
- glycerophosphohydrolase


entry: 3.1.4.3
sysname: phosphatidylcholine cholinephosphohydrolase
reaction: A phosphatidylcholine + H2O = 1,2-diacylglycerol + choline phosphate [RN:R01312]
iubmb_reaction: R01312
kegg_reaction: R02027 R02052 R03332 R07381
name:
--- 
- phospholipase C
- lipophosphodiesterase I
- lecithinase C
- Clostridium welchii alpha-toxin
- Clostridium oedematiens beta- and gamma-toxins
- lipophosphodiesterase C
- phosphatidase C
- heat-labile hemolysin
- alpha-toxin

comment:
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.


entry: 3.1.4.8
name: --- - Transferred to 3.1.27.3
comment:
Transferred entry: now EC 3.1.27.3 ribonuclease T1 (EC 3.1.4.8 created 1961, transferred 1965 to EC 2.7.7.26, reinstated 1972, deleted 1978)


entry: 3.1.4.9
name: --- - Transferred to 3.1.30.2
comment:
Transferred entry: now EC 3.1.30.2 Serratia marcescens nuclease (EC 3.1.4.9 created 1965, deleted 1978)


entry: 3.1.4.10
name: --- - Transferred to 4.6.1.13
comment:
Transferred entry: now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase. As there is no hydrolysis of the inositol 1,2-cyclic phosphate formed, previous classification of the enzyme as a hydrolase was incorrect. (EC 3.1.4.10 created 1972, modified 1976, deleted 2002)


entry: 3.1.4.11
sysname: 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
iubmb_reaction: (other) R03435
kegg_reaction: R03435
name:
--- 
- phosphoinositide phospholipase C
- triphosphoinositide phosphodiesterase
- phosphoinositidase C
- 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
- monophosphatidylinositol phosphodiesterase
- phosphatidylinositol phospholipase C
- PI-PLC
- 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase

comment:
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four beta-isoforms regulated by G-proteins, two gamma-forms regulated by tyrosine kinases, four delta-forms regulated at least in part by calcium and an epsilon-form, probably regulated by the oncogene ras, have been found.

reaction:
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol


entry: 3.1.4.13
sysname: serine-phosphoethanolamine ethanolaminephosphohydrolase
comment: Acts only on those phosphodiesters that have ethanolamine as a component part of the molecule.
reaction: serine phosphoethanolamine + H2O = serine + ethanolamine phosphate [RN:R02817]
iubmb_reaction: R02817
name:
--- 
- serine-ethanolaminephosphate phosphodiesterase
- serine ethanolamine phosphodiester phosphodiesterase
- SEP diesterase


entry: 3.1.4.14
sysname: holo-[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase
reaction: holo-[acyl-carrier-protein] + H2O = 4'-phosphopantetheine + apo-[acyl-carrier-protein] [RN:R01623]
iubmb_reaction: R01623
name:
--- 
- "[acyl-carrier-protein] phosphodiesterase"
- ACP hydrolyase
- ACP phosphodiesterase
- AcpH
- "[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase"

comment:
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier-protein (ACP) and short-chain ACPs over the medium- and long-chain species [3]. Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo [3]. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase.


entry: 3.1.4.15
sysname: adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] adenylylhydrolase
iubmb_reaction: R03474
name:
--- 
- adenylyl-[glutamate-ammonia ligase] hydrolase
- adenylyl-[glutamine-synthetase]hydrolase
- adenylyl(glutamine synthetase) hydrolase

reaction:
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O = adenylate + [L-glutamate:ammonia ligase (ADP-forming)] [RN:R03474]


entry: 3.1.4.16
sysname: nucleoside-2',3'-cyclic-phosphate 3'-nucleotidohydrolase
reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate [RN:R03423]
iubmb_reaction: R03423 > R03537 R03538 R03929 R05135
name:
--- 
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase
- ribonucleoside 2',3'-cyclic phosphate diesterase
- 2',3 '-cyclic AMP phosphodiesterase
- 2',3'-cyclic nucleotidase
- cyclic 2',3'-nucleotide 2'-phosphodiesterase
- cyclic 2',3'-nucleotide phosphodiesterase
- 2',3'-cyclic nucleoside monophosphate phosphodiesterase
- 2',3'-cyclic AMP 2'-phosphohydrolase
- cyclic phosphodiesterase:3'-nucleotidase
- 2',3'-cyclic nucleotide phosphohydrolase
- 2':3'-cyclic phosphodiesterase
- 2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase

comment:
Also hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides. Similar reactions are carried out by EC 3.1.27.3 (ribonuclease T1) and EC 3.1.27.5 (pancreatic ribonuclease).


entry: 3.1.4.17
sysname: 3',5'-cyclic-nucleotide 5'-nucleotidohydrolase
reaction: nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
iubmb_reaction: R03259 > R00191 R01234
name:
--- 
- 3',5'-cyclic-nucleotide phosphodiesterase
- cyclic 3',5'-mononucleotide phosphodiesterase
- PDE
- cyclic 3',5'-nucleotide phosphodiesterase
- cyclic 3',5'-phosphodiesterase
- 3',5'-nucleotide phosphodiesterase
- 3':5'-cyclic nucleotide 5'-nucleotidohydrolase
- 3',5'-cyclonucleotide phosphodiesterase
- cyclic nucleotide phosphodiesterase
- 3', 5'-cyclic nucleoside monophosphate phosphodiesterase
- "3': 5'-monophosphate phosphodiesterase (cyclic CMP)"
- cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP)
- cyclic 3',5-nucleotide monophosphate phosphodiesterase
- nucleoside 3',5'-cyclic phosphate diesterase
- nucleoside-3',5-monophosphate phosphodiesterase

comment:
Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.


entry: 3.1.4.27
name: --- - Transferred to 3.1.11.2
comment:
Transferred entry: now EC 3.1.11.2 exodeoxyribonuclease III (EC 3.1.4.27 created 1972, deleted 1978)


entry: 3.1.4.28
name: --- - Transferred to 3.1.11.3
comment:
Transferred entry: now EC 3.1.11.3 exodeoxyribonuclease (lambda-induced) (EC 3.1.4.28 created 1972, deleted 1978)


entry: 3.1.4.30
name: --- - Transferred to 3.1.21.2
comment:
Transferred entry: now EC 3.1.21.2 deoxyribonuclease IV (phage T4-induced) (EC 3.1.4.30 created 1972, deleted 1978)


entry: 3.1.4.31
name: --- - Transferred to 3.1.11.4
comment:
Transferred entry: now EC 3.1.11.4 exodeoxyribonuclease (phage SP3-induced) (EC 3.1.4.31 created 1972, deleted 1978)


entry: 3.1.4.32
name: --- - Deleted entry
comment:
Deleted entry: endodeoxyribonuclease (ATP- and S-adenosylmethionine-dependent). See EC 3.1.21.3 type 1 site-specific deoxyribonuclease and EC 3.1.21.5 type III site-specific deoxyribonuclease (EC 3.1.4.32 created 1972, deleted 1978)


entry: 3.1.4.33
name: --- - Deleted entry
comment:
Deleted entry: endodeoxyribonuclease (ATP-hydrolysing). See EC 3.1.21.3 type 1 site-specific deoxyribonuclease and EC 3.1.21.5 type III site-specific deoxyribonuclease (EC 3.1.4.33 created 1972, deleted 1978)


entry: 3.1.4.34
name: --- - Deleted entry
comment:
Deleted entry: hybrid nuclease. See subclasses EC 3.1.15, EC 3.1.16, EC 3.1.30 and EC 3.1.31 (EC 3.1.4.34 created 1972, deleted 1978)


entry: 3.1.4.35
sysname: 3',5'-cyclic-GMP 5'-nucleotidohydrolase
reaction: guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
iubmb_reaction: R01234
name:
--- 
- 3',5'-cyclic-GMP phosphodiesterase
- guanosine cyclic 3',5'-phosphate phosphodiesterase
- cyclic GMP phosphodiesterase
- cyclic 3',5'-GMP phosphodiesterase
- cyclic guanosine 3',5'-monophosphate phosphodiesterase
- cyclic guanosine 3',5'-phosphate phosphodiesterase
- cGMP phosphodiesterase
- cGMP-PDE


entry: 3.1.4.36
name: --- - Deleted entry
comment:
Deleted entry: 1,2-cyclic-inositol-phosphate phosphodiesterase. Now included with EC 3.1.4.43, glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.36 created 1976, deleted 2002)


entry: 3.1.4.37
sysname: nucleoside-2',3'-cyclic-phosphate 2'-nucleotidohydrolase
reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate [RN:R03422]
iubmb_reaction: R03422
name:
--- 
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- cyclic-CMP phosphodiesterase
- 2',3'-cyclic AMP phosphodiesterase
- cyclic 2',3'-nucleotide 3'-phosphodiesterase
- cyclic 2',3'-nucleotide phosphodiesterase
- 2',3'-cyclic nucleoside monophosphate phosphodiesterase
- 2',3'-cyclic nucleotide 3'-phosphohydrolase
- CNPase
- 2',3'-cyclic nucleotide phosphohydrolase
- 2':3'-cyclic nucleotide 3'-phosphodiesterase
- 2':3'-CNMP-3'-ase

comment:
The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3',5'-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase.


entry: 3.1.4.38
sysname: sn-glycero-3-phosphocholine cholinephosphohydrolase
comment: No activity on sn-3-glycerophosphoethanolamine.
reaction: sn-glycero-3-phosphocholine + H2O = glycerol + choline phosphate [RN:R02591]
iubmb_reaction: R02591
name:
--- 
- glycerophosphocholine cholinephosphodiesterase
- L-3-glycerylphosphinicocholine cholinephosphohydrolase


entry: 3.1.4.39
name: --- - alkylglycerophosphoethanolamine phosphodiesterase - lysophospholipase D
sysname: 1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase
comment: Also acts on acyl and choline analogues.
iubmb_reaction: R04362
kegg_reaction: R07388
reaction:
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine [RN:R04362]


entry: 3.1.4.40
sysname: CMP-N-acylneuraminate N-acylneuraminohydrolase
reaction: CMP-N-acylneuraminate + H2O = CMP + N-acylneuraminate [RN:R02598]
iubmb_reaction: R02598
name:
--- 
- CMP-N-acylneuraminate phosphodiesterase
- CMP-sialate hydrolase
- CMP-sialic acid hydrolase
- CMP-N-acylneuraminic acid hydrolase
- cytidine monophosphosialic hydrolase
- cytidine monophosphosialate hydrolase
- cytidine monophosphate-N-acetylneuraminic acid hydrolase
- CMP-N-acetylneuraminate hydrolase


entry: 3.1.4.41
name: --- - sphingomyelin phosphodiesterase D - sphingomyelinase D
sysname: sphingomyelin ceramide-phosphohydrolase
reaction: sphingomyelin + H2O = ceramide phosphate + choline [RN:R02542]
iubmb_reaction: R02542
comment:
Does not act on phosphatidylcholine, but hydrolyses 2-lysophosphatidylcholine to choline and 2-lysophosphatidate.


entry: 3.1.4.42
sysname: rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase
reaction: glycerol 1,2-cyclic phosphate + H2O = glycerol 1-phosphate [RN:R02648]
iubmb_reaction: R02648
name:
--- 
- glycerol-1,2-cyclic-phosphate 2-phosphodiesterase
- rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase

comment:
Acts on both stereoisomers of the substrate and also, more slowly, on 3',5'-cyclic AMP and on 2',3'-cyclic AMP.


entry: 3.1.4.43
sysname: 1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase
comment: This enzyme also hydrolyses Ins(cyclic 1,2)P to Ins-1-P
reaction: 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = glycerol + 1D-myo-inositol 1-phosphate [RN:R03331]
iubmb_reaction: R03331
kegg_reaction: R03333
name:
--- 
- glycerophosphoinositol inositolphosphodiesterase
- 1,2-cyclic-inositol-phosphate phosphodiesterase
- D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase
- D-inositol 1,2-cyclic phosphate 2-phosphohydrolase
- D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase
- 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase
- inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase


entry: 3.1.4.44
sysname: 1-(sn-glycero-3-phospho)-1D-myo-inositol glycerophosphohydrolase
reaction: 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate [RN:R01193]
iubmb_reaction: R01193
name:
--- 
- glycerophosphoinositol glycerophosphodiesterase
- sn-glycero(3)phosphoinositol glycerophosphohydrolase
- sn-glycero-3-phospho-1-inositol glycerophosphohydrolase


entry: 3.1.4.45
sysname: glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase
iubmb_reaction: R04373
name:
--- 
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- alpha-N-acetylglucosaminyl phosphodiesterase
- lysosomal alpha-N-acetylglucosaminidase
- phosphodiester glycosidase
- alpha-N-acetyl-D-glucosamine-1-phosphodiester N-acetylglucosaminidase
- 2-acetamido-2-deoxy-alpha-D-glucose 1-phosphodiester acetamidodeoxyglucohydrolase

comment:
Acts on a variety of compounds in which N-acetyl-D-glucosamine is alpha-linked to a phosphate group, including the biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the products of EC 2.7.8.17 UDP-N-acetylglucosamine#151;lysosomal-enzyme N-acetylglucosaminephosphotransferase.

reaction:
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose [RN:R04373]


entry: 3.1.4.46
sysname: glycerophosphodiester glycerophosphohydrolase
reaction: A glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate [RN:R00857]
iubmb_reaction: R00857 > R01030 R01470
name:
--- 
- glycerophosphodiester phosphodiesterase
- gene hpd protein
- glycerophosphoryl diester phosphodiesterase
- IgD-binding protein D

comment:
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.


entry: 3.1.4.47
name: --- - Transferred to 4.6.1.14
comment:
Transferred entry: now EC 4.6.1.14, glycosylphosphatidylinositol diacylglycerol-lyase (EC 3.1.4.47 created 1989, deleted 2002)


entry: 3.1.4.48
sysname: dolichyl-beta-D-glucosyl-phosphate dolichylphosphohydrolase
reaction: dolichyl beta-D-glucosyl phosphate + H2O = dolichyl phosphate + D-glucose [RN:R01006]
iubmb_reaction: R01006
name:
--- 
- dolichylphosphate-glucose phosphodiesterase
- dolichol phosphoglucose phosphodiesterase
- Dol-P-Glc phosphodiesterase


entry: 3.1.4.50
sysname: glycoprotein-phosphatidylinositol phosphatidohydrolase
iubmb_reaction: R06623(G)
kegg_reaction: R04149 R07398
name:
--- 
- glycosylphosphatidylinositol phospholipase D
- GPI-PLD
- glycoprotein phospholipase D
- phosphatidylinositol phospholipase D
- phosphatidylinositol-specific phospholipase D

comment:
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.

reaction:
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate [RN:R06623]


entry: 3.1.4.51
sysname: 6-(D-glucose-1-phospho)-D-mannosylglycoprotein glucose-1-phosphohydrolase
iubmb_reaction: R04180
name:
--- 
- glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase
- alpha-glucose-1-phosphate phosphodiesterase

comment:
The enzyme is specific for the product of EC 2.7.8.19 UDP-glucose-glycoprotein glucose phosphotransferase.

reaction:
6-(D-glucose-1-phospho)-D-mannosylglycoprotein + H2O = alpha-D-glucose 1-phosphate + D-mannosylglycoprotein [RN:R04180]


entry: 3.1.4.-
name: --- []
reaction:
(1) N-Acetyl-D-mannosamine + UDP <=> UDP-N-acetyl-D-mannosamine + H2O [RN:R02707]; (2) 1-(1-Alkenyl)-sn-glycero-3-phosphoethanolamine + H2O <=> 1-(1-Alkenyl)-sn-glycerol + Ethanolamine phosphate [RN:R07380]


entry: 3.1.5.1
sysname: dGTP triphosphohydrolase
comment: Also acts on GTP.
reaction: dGTP + H2O = deoxyguanosine + triphosphate [RN:R01856]
iubmb_reaction: R01856
name:
--- 
- dGTPase
- deoxy-GTPase
- deoxyguanosine 5-triphosphate triphosphohydrolase
- deoxyguanosine triphosphatase
- deoxyguanosine triphosphate triphosphohydrolase


entry: 3.1.6.1
sysname: aryl-sulfate sulfohydrolase
comment: A group of enzymes with rather similar specificities.
reaction: A phenol sulfate + H2O = a phenol + sulfate [RN:R01243]
iubmb_reaction: R01243 > R03980
kegg_reaction: R04856 R06280(G)
name:
--- 
- arylsulfatase
- sulfatase
- nitrocatechol sulfatase
- phenolsulfatase
- phenylsulfatase
- p-nitrophenyl sulfatase
- arylsulfohydrolase
- 4-methylumbelliferyl sulfatase
- estrogen sulfatase
- arylsulfatase C
- arylsulfatase B
- arylsulfatase A


entry: 3.1.6.2
sysname: steryl-sulfate sulfohydrolase
comment: Also acts on some related steryl sulfates.
iubmb_reaction: R03404
name:
--- 
- steryl-sulfatase
- arylsulfatase
- steroid sulfatase
- sterol sulfatase
- dehydroepiandrosterone sulfate sulfatase
- arylsulfatase C
- steroid 3-sulfatase
- steroid sulfate sulfohydrolase
- dehydroepiandrosterone sulfatase
- pregnenolone sulfatase
- phenolic steroid sulfatase
- 3-beta-hydroxysteroid sulfate sulfatase

reaction:
3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate [RN:R03404]


entry: 3.1.6.4
sysname: N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase
name:
--- 
- N-acetylgalactosamine-6-sulfatase
- chondroitin sulfatase
- chondroitinase
- galactose-6-sulfate sulfatase
- acetylgalactosamine 6-sulfatase
- N-acetylgalactosamine-6-sulfate sulfatase
- N-acetylgalactosamine 6-sulfatase

reaction:
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate


entry: 3.1.6.8
name: --- - cerebroside-sulfatase - arylsulfatase A - cerebroside sulfate sulfatase
sysname: cerebroside-3-sulfate 3-sulfohydrolase
reaction: A cerebroside 3-sulfate + H2O = a cerebroside + sulfate [RN:R04856 R06280]
iubmb_reaction: R04856 R06280(G)
comment:
Hydrolyses galactose-3-sulfate residues in a number of lipids. Also hydrolyses ascorbate 2-sulfate and many phenol sulfates.


entry: 3.1.6.9
name: --- - chondro-4-sulfatase - chondroitin-4-sulfatase
sysname: 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-4-su lfate 4-sulfohydrolase
comment: Also acts on the saturated analogue but not on higher oligosaccharides, nor any 6-sulfates.
iubmb_reaction: R03517
reaction:
4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate + H2O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine + sulfate [RN:R03517]


entry: 3.1.6.10
name: --- - chondro-6-sulfatase
sysname: 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-6-su lfate 6-sulfohydrolase
iubmb_reaction: R03518
comment:
Also acts on the saturated analogue and N-acetyl-D-galactosamine 4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate

reaction:
4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 6-sulfate + H2O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine + sulfate [RN:R03518]


entry: 3.1.6.11
sysname: N,6-O-disulfo-D-glucosamine 6-sulfohydrolase
comment: May be identical with EC 3.1.6.14 N-acetylglucosamine-6-sulfatase.
reaction: N,6-O-disulfo-D-glucosamine + H2O = N-sulfo-D-glucosamine + sulfate [RN:R03216]
iubmb_reaction: R03216
name:
--- 
- disulfoglucosamine-6-sulfatase
- N-sulfoglucosamine-6-sulfatase
- 6,N-disulfoglucosamine 6-O-sulfohydrolase


entry: 3.1.6.12
sysname: N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase
comment: Acts also on N-acetylglucosamine 4-sulfate.
name:
--- 
- N-acetylgalactosamine-4-sulfatase
- chondroitinsulfatase
- chondroitinase
- arylsulfatase B
- acetylgalactosamine 4-sulfatase
- N-acetylgalactosamine 4-sulfate sulfohydrolase

reaction:
Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate


entry: 3.1.6.13
sysname: L-iduronate-2-sulfate 2-sulfohydrolase
name:
--- 
- iduronate-2-sulfatase
- chondroitinsulfatase
- idurono-2-sulfatase
- iduronide-2-sulfate sulfatase
- L-iduronosulfatase
- L-idurono sulfate sulfatase
- iduronate sulfatase
- sulfo-L-iduronate sulfatase
- L-iduronate 2-sulfate sulfatase
- sulfoiduronate sulfohydrolase
- 2-sulfo-L-iduronate 2-sulfatase
- iduronate-2-sulfate sulfatase
- iduronate sulfate sulfatase

reaction:
Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin


entry: 3.1.6.14
sysname: N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase
comment: May be identical with EC 3.1.6.11 disulfoglucosamine-6-sulfatase.
name:
--- 
- N-acetylglucosamine-6-sulfatase
- chondroitinsulfatase
- O,N-disulfate O-sulfohydrolase
- acetylglucosamine 6-sulfatase
- N-acetylglucosamine 6-sulfate sulfatase
- 2-acetamido-2-deoxy-D-glucose 6-sulfate sulfatase

reaction:
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate


entry: 3.1.6.15
name: --- - N-sulfoglucosamine-3-sulfatase - chondroitinsulfatase
sysname: N-sulfo-3-sulfoglucosamine 3-sulfohydrolase
reaction: Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin
comment:
The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue.


entry: 3.1.6.18
name: --- - glucuronate-2-sulfatase - glucurono-2-sulfatase
sysname: polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase
comment: Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13 iduronate-2-sulfatase)
reaction:
Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate


entry: 3.1.7.2
sysname: guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
reaction: guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate [RN:R00336]
iubmb_reaction: R00336
name:
--- 
- guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
- guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase
- PpGpp-3'-pyrophosphohydrolase
- PpGpp phosphohydrolase


entry: 3.1.7.3
name: --- - monoterpenyl-diphosphatase - bornyl pyrophosphate hydrolase - monoterpenyl-pyrophosphatase
sysname: monoterpenyl-diphosphate diphosphohydrolase
reaction: monoterpenyl diphosphate + H2O = monoterpenol + diphosphate [RN:R03016]
iubmb_reaction: R03016
comment:
A group of enzymes with varying specificity for the monoterpenol moiety. One has the highest activity on sterically hindered compounds such as (+)-bornyl diphosphate; another has highest activity on the diphosphates of primary allylic alcohols such as geraniol.


entry: 3.1.8.1
sysname: aryltriphosphate dialkylphosphohydrolase
reaction: An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]
iubmb_reaction: R03979
kegg_reaction: R05421 R05548
name:
--- 
- aryldialkylphosphatase
- organophosphate hydrolase
- paraoxonase
- A-esterase
- aryltriphosphatase
- organophosphate esterase
- esterase B1
- esterase E4
- paraoxon esterase
- pirimiphos-methyloxon esterase
- OPA anhydrase
- organophosphorus hydrolase
- phosphotriesterase
- paraoxon hydrolase
- OPH
- organophosphorus acid anhydrase

comment:
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.


entry: 3.1.8.2
sysname: diisopropyl-fluorophosphate fluorohydrolase
reaction: diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride [RN:R01533]
iubmb_reaction: R01533
name:
--- 
- diisopropyl-fluorophosphatase
- DFPase
- tabunase
- somanase
- organophosphorus acid anhydrolase
- organophosphate acid anhydrase
- OPA anhydrase
- diisopropylphosphofluoridase
- dialkylfluorophosphatase
- diisopropyl phosphorofluoridate hydrolase
- isopropylphosphorofluoridase
- diisopropylfluorophosphonate dehalogenase

comment:
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase. Previously listed as EC 3.8.2.1.


entry: 3.1.11.1
reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
name:
--- 
- exodeoxyribonuclease I
- Escherichia coli exonuclease I
- E. coli exonuclease I
- exonuclease I

comment:
Preference for single-stranded DNA. The Escherichia coli enzyme hydrolyses glucosylated DNA. Formerly EC 3.1.4.25.


entry: 3.1.11.2
reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
name:
--- 
- exodeoxyribonuclease III
- Escherichia coli exonuclease III
- E. coli exonuclease III
- endoribonuclease III

comment:
Preference for double-stranded DNA. Has endonucleolytic activity near apurinic sites on DNA. Formerly EC 3.1.4.27.


entry: 3.1.11.3
comment: Preference for double-stranded DNA. Does not attack single-strand breaks. Formerly EC 3.1.4.28.
reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates
name:
--- 
- exodeoxyribonuclease (lambda-induced)
- lambda exonuclease
- phage lambda-induced exonuclease
- Escherichia coli exonuclease IV
- E. coli exonuclease IV
- exodeoxyribonuclease IV
- exonuclease IV


entry: 3.1.11.4
comment: Preference for single-stranded DNA. Formerly EC 3.1.4.31.
reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates
name:
--- 
- exodeoxyribonuclease (phage SP3-induced)
- phage SP3 DNase
- DNA 5'-dinucleotidohydrolase
- deoxyribonucleate 5'-dinucleotidase
- deoxyribonucleic 5'-dinucleotidohydrolase
- bacteriophage SP3 deoxyribonuclease


entry: 3.1.11.5
name:
--- 
- exodeoxyribonuclease V
- Escherichia coli exonuclease V
- E. coli exonuclease V
- gene recBC endoenzyme
- RecBC deoxyribonuclease
- gene recBC DNase
- exonuclease V
- gene recBCD enzymes

comment:
Preference for double-stranded DNA. Possesses DNA-dependent ATPase activity. Acts endonucleolytically on single-stranded circular DNA.

reaction:
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides


entry: 3.1.11.6
comment: Preference for single-stranded DNA.
name:
--- 
- exodeoxyribonuclease VII
- Escherichia coli exonuclease VII
- E. coli exonuclease VII
- endodeoxyribonuclease VII
- exonuclease VII

reaction:
Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates


entry: 3.1.13.1
reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
name:
--- 
- exoribonuclease II
- ribonuclease II
- ribonuclease Q
- BN ribonuclease
- Escherichia coli exo-RNase II
- RNase II
- exoribonuclease
- 5'-exoribonuclease

comment:
Preference for single-stranded RNA. The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5 ribonuclease P. Formerly EC 3.1.4.20.


entry: 3.1.13.2
name: --- - exoribonuclease H - retroviral reverse transcriptase RNaseH
comment: Attacks RNA in duplex with DNA strand. Found in certain oncorna viruses and animal cells.
reaction:
Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in both 5'- to 3'- and 3'- to 5'- directions


entry: 3.1.13.5
name: --- - ribonuclease D - RNase D
comment:
Requires divalent cations for activity (Mg2+, Mn2+ or Co2+). Alteration of the 3'-terminal base has no effect on the rate of hydrolysis whereas modification of the 3'-terminal sugar has a major effect. tRNA terminating with a 3'-phosphate is completely inactive [3]. This enzyme can convert a tRNA precursor into a mature tRNA [2].

reaction:
Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides


entry: 3.1.16.1
reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates
name:
--- 
- spleen exonuclease
- 3'-exonuclease
- spleen phosphodiesterase
- 3'-nucleotide phosphodiesterase
- phosphodiesterase II

comment:
Preference for single-stranded substrate. Formerly EC 3.1.4.18 (cf. EC 3.1.31.1 micrococcal nuclease).


entry: 3.1.21.1
comment: Preference for double-stranded DNA. Formerly EC 3.1.4.5.
reaction: Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
name:
--- 
- deoxyribonuclease I
- pancreatic DNase
- DNase
- thymonuclease, dornase
- dornava
- dornavac
- pancreatic deoxyribonuclease
- pancreatic dornase
- deoxyribonuclease (pancreatic)
- DNAase
- deoxyribonucleic phosphatase
- DNase I
- alkaline deoxyribonuclease
- alkaline DNase
- endodeoxyribonuclease I
- DNA depolymerase
- Escherichia coli endonuclease I
- deoxyribonuclease A
- DNA endonuclease
- DNA nuclease


entry: 3.1.21.2
comment: Preference for single-stranded DNA. Formerly EC 3.12.4.30.
reaction: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products
name:
--- 
- deoxyribonuclease IV (phage-T4-induced)
- endodeoxyribonuclease IV (phage T4-induced)
- E. coli endonuclease IV
- endodeoxyribonuclease
- redoxyendonuclease
- deoxriboendonuclease
- Escherichia coli endonuclease II
- endonuclease II
- DNA-adenine-transferase


entry: 3.1.21.3
name:
--- 
- type I site-specific deoxyribonuclease
- type I restriction enzyme
- deoxyribonuclease (ATP- and S-adenosyl-L-methionine-dependent)
- restriction-modification system
- deoxyribonuclease (adenosine triphosphate-hydrolyzing)
- adenosine triphosphate-dependent deoxyribonuclease
- ATP-dependent DNase
- type 1 site-specific deoxyribonuclease

comment:
This is a large group of enzymes which, together with those now listed as EC 3.1.21.4 (type II site-specific deoxyribonuclease) and EC 3.1.21.5 (type III site-specific deoxyribonuclease), were previously listed separately in sub-subclasses EC 3.1.23 and EC 3.1.24. They have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence. They are multifunctional proteins that also catalyse the reactions of EC 2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)] and EC 2.1.1.37 [DNA (cytosine-5-)-methyltransferase], with similar site specificity. A complete listing of all of these enzymes has been produced by R.J. Roberts and is available at http://rebase.neb.com/rebase/rebase.html

reaction:
Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolysed


entry: 3.1.21.4
name: --- - type II site-specific deoxyribonuclease - type II restriction enzyme
comment:
This is a large group of enzymes which, together with those now listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease) and EC 3.1.21.5 (type III site-specific deoxyribonuclease), were previously listed separately in sub-subclasses 3.1.23 and 3.1.24. They require only Mg2+. They recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site. A complete listing of all of these enzymes has been produced by R.J. Roberts and is available at http://rebase.neb.com/rebase/rebase.html.

reaction:
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates


entry: 3.1.21.5
name:
--- 
- type III site-specific deoxyribonuclease
- type III restriction enzyme
- restriction-modification system

comment:
This is a large group of enzymes which, together with those now listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease) and EC 3.1.21.4 (type II site-specific deoxyribonuclease), were previously listed separately in sub-subclasses EC 3.1.23 and EC 3.1.24. They have an absolute requirement for ATP but do not hydrolyse it; S-adenosy-L-methionine stimulates the reaction, but is not absolutely required. They recognize specific, short DNA sequences and cleave a short distance away from the recognition sequence. These enzymes exist as complexes with enzymes of similar specificity listed under EC 2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)] or EC 2.1.1.73 [site-specific DNA-methyltransferase (cytosine-specific)]. A complete listing of all of these enzymes has been produced by R.J. Roberts and is available at http://rebase.neb.com/rebase/rebase.html

reaction:
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates


entry: 3.1.21.6
name:
--- 
- CC-preferring endodeoxyribonuclease
- Streptomyces glaucescens exocytoplasmic dodeoxyribonuclease

comment:
prefers CC sites in double-stranded circular and linear DNA. Greater affinity for double-stranded than single-stranded DNA. Produces nicks, generating double-stranded fragments with 5'- and/or 3'-protruding single-stranded tails. Requires magnesium ions for activity. The endonuclease from Chlorella-like green algae infected with NYs-1 virus 4[1] may be the same enzyme.

reaction:
endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC


entry: 3.1.21.7
comment: Previously classified erroneously as EC 3.1.22.3.
reaction: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate
name:
--- 
- deoxyribonuclease V
- endodeoxyribonuclease V
- DNase V
- Escherichia coli endodeoxyribonuclease V


entry: 3.1.22.1
comment: Preference for double-stranded DNA. Formerly EC 3.1.4.6.
reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
name:
--- 
- deoxyribonuclease II
- DNase II
- pancreatic DNase II
- deoxyribonucleate 3'-nucleotidohydrolase
- acid deoxyribonuclease
- acid DNase


entry: 3.1.22.4
name:
--- 
- crossover junction endodeoxyribonuclease
- Hje endonuclease
- Holliday junction endonuclease CCE1
- Holliday junction resolvase
- Holliday junction-cleaving endonuclease
- Holliday junction-resolving endoribonuclease
- RusA Holliday junction resolvase
- RusA endonuclease
- RuvC endonuclease
- SpCCe1 Holliday junction resolvase
- crossover junction endoribonuclease
- cruciform-cutting endonuclease
- endo X3
- endonuclease RuvC
- endonuclease VII
- endonuclease X3
- resolving enzyme CCE1

comment:
The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions.

reaction:
Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction)


entry: 3.1.22.5
reaction: Endonucleolytic cleavage of supercoiled plasma DNA to linear DNA duplexes
name:
--- 
- deoxyribonuclease X
- Escherichia coli endodeoxyribonuclease
- Escherichia coli endodeoxyribonuclease X

comment:
Preference for supercoiled DNA; little activity on linear double-stranded DNA. Inhibited by single-stranded DNA, ATP and AMP.


entry: 3.1.25.1
comment: Acts on a damaged strand, 5' from the damaged site.
reaction: Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate
name:
--- 
- deoxyribonuclease (pyrimidine dimer)
- endodeoxyribonuclease (pyrimidine dimer)
- bacteriophage T4 endodeoxyribonuclease V
- T4 endonuclease V


entry: 3.1.25.2
name: --- - Transferred to 4.2.99.18
comment:
Transferred entry: now EC 4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.25.2 created 1978, deleted 1992)


entry: 3.1.26.3
name: --- - ribonuclease III - RNase III - ribonuclease 3
reaction: Endonucleolytic cleavage to a 5'-phosphomonoester
comment:
This is an endoribonuclease that cleaves double-stranded RNA molecules [4]. The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site [5]. Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage [6]. RNase III is involved in both rRNA processing and mRNA processing and decay.


entry: 3.1.26.4
comment: Acts on RNA-DNA hybrids.
reaction: Endonucleolytic cleavage to 5'-phosphomonoester
name:
--- 
- calf thymus ribonuclease H
- endoribonuclease H (calf thymus)
- RNase H
- RNA*DNA hybrid ribonucleotidohydrolase
- hybrid ribonuclease
- hybridase
- hybridase (ribonuclease H)
- ribonuclease H
- hybrid nuclease


entry: 3.1.26.5
name: --- - ribonuclease P - RNase P
reaction: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
comment:
An RNA-containing enzyme, essential for tRNA processing; generates 5'-termini or mature tRNA molecules.


entry: 3.1.26.8
name:
--- 
- ribonuclease M5
- RNase M5
- 5S ribosomal maturation nuclease
- 5S ribosomal RNA maturation endonuclease

comment:
Converts the 5S-rRNA precursor from Bacillus subtilis into 5S-rRNA, with 5'-phosphate and 3'-hydroxy groups.

reaction:
Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor


entry: 3.1.26.9
comment: Forms oligonucleotides with chain lengths of 6 to 12.
reaction: Endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups
name:
--- 
- ribonuclease [poly-(U)-specific]
- ribonuclease (uracil-specific)
- uracil-specific endoribonuclease
- uracil-specific RNase


entry: 3.1.26.10
name: --- - ribonuclease IX - poly(U)- and poly(C)-specific endoribonuclease
comment:
Acts on poly(U) and poly(C), with a higher affinity for poly(C), but does not act on poly(A) or poly(G).

reaction:
Endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups


entry: 3.1.26.11
name: --- - tRNase Z - 3 tRNase - tRNA 3 endonuclease - RNase Z - 3' tRNase
comment:
No cofactor requirements. An homologous enzyme to that found in Arabidopsis thaliana has been found in Methanococcus janaschii.

reaction:
endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule


entry: 3.1.27.1
comment: Formerly EC 2.7.7.17 and EC 3.1.4.23.
name:
--- 
- ribonuclease T2
- ribonuclease II
- base-non-specific ribonuclease
- nonbase-specific RNase
- RNase (non-base specific)
- non-base specific ribonuclease
- nonspecific RNase
- RNase Ms
- RNase M
- RNase II
- Escherichia coli ribonuclease II
- ribonucleate nucleotido-2'-transferase (cyclizing)
- acid ribonuclease
- RNAase CL
- Escherichia coli ribonuclease I' ribonuclease PP2
- ribonuclease N2
- ribonuclease M
- acid RNase
- ribonnuclease (non-base specific)
- ribonuclease (non-base specific)
- RNase T2
- ribonuclease PP3
- ribonucleate 3'-oligonucleotide hydrolase
- ribonuclease U4

reaction:
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates


entry: 3.1.27.2
reaction: Endonucleolytic cleavage to 2',3'-cyclic nucleotides
name:
--- 
- Bacillus subtilis ribonuclease
- Proteus mirabilis RNase
- ribonucleate nucleotido-2'-transferase (cyclizing)


entry: 3.1.27.3
comment: Formerly EC 2.7.7.26 and EC 3.1.4.8.
name:
--- 
- ribonuclease T1
- guanyloribonuclease
- Aspergillus oryzae ribonuclease
- RNase N1
- RNase N2
- ribonuclease N3
- ribonuclease U1
- ribonuclease F1
- ribonuclease Ch
- ribonuclease PP1
- ribonuclease SA
- RNase F1
- ribonuclease C2
- binase
- RNase Sa
- guanyl-specific RNase
- RNase G
- RNase T1
- ribonuclease guaninenucleotido-2'-transferase (cyclizing)
- ribonuclease N1

reaction:
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Gp with 2',3'-cyclic phosphate intermediates


entry: 3.1.27.4
name:
--- 
- ribonuclease U2
- purine specific endoribonuclease
- ribonuclease U3
- RNase U3
- RNase U2
- purine-specific ribonuclease
- purine-specific RNase
- Pleospora RNase
- Trichoderma koningi RNase III
- ribonuclease (purine)

reaction:
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates


entry: 3.1.27.5
comment: Formerly EC 2.7.7.16 and EC 3.1.4.22.
name:
--- 
- pancreatic ribonuclease
- RNase
- RNase I
- RNase A
- pancreatic RNase
- ribonuclease I
- endoribonuclease I
- ribonucleic phosphatase
- alkaline ribonuclease
- ribonuclease
- gene S glycoproteins
- Ceratitis capitata alkaline ribonuclease
- SLSG glycoproteins
- gene S locus-specific glycoproteins
- S-genotype-asssocd. glycoproteins
- ribonucleate 3'-pyrimidino-oligonucleotidohydrolase

reaction:
Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates


entry: 3.1.27.6
name: --- - Enterobacter ribonuclease
comment: Preference for cleavage at CpA. Homopolymers of A, U or G are not hydrolysed.
reaction:
Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates


entry: 3.1.27.9
comment: The enzyme catalyses the final stage in the maturation of tRNA molecules.
name:
--- 
- tRNA-intron endonuclease
- transfer ribonucleate intron endoribonuclease
- tRNA splicing endonuclease
- splicing endonuclease
- tRNATRPintron endonuclease
- transfer splicing endonuclease

reaction:
Endonucleolytic cleavage of pre-tRNA, producing 5'-hydroxy and 2',3'-cyclic phosphate termini, and specifically removing the intron


entry: 3.1.27.10
name: --- - rRNA endonuclease - alpha-sarcin
comment: Also acts on bacterial rRNA.
reaction:
Hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes


entry: 3.1.30.1
comment: Formerly EC 3.1.4.21.
reaction: Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
name:
--- 
- Aspergillus nuclease S1
- endonuclease S1 (Aspergillus)
- single-stranded-nucleate endonuclease
- deoxyribonuclease S1
- nuclease S1
- Neurospora crassa single-strand specific endonuclease
- S1 nuclease
- single-strand endodeoxyribonuclease
- single-stranded DNA specific endonuclease
- single-strand-specific endodeoxyribonuclease
- single strand-specific DNase
- Aspergillus oryzae S1 nuclease


entry: 3.1.30.2
comment: Hydrolyses double- or single-stranded substrate. Formerly EC 3.1.4.9.
reaction: Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
name:
--- 
- Serratia marcescens nuclease
- endonuclease (Serratia marcescens)
- barley nuclease
- plant nuclease I
- nucleate endonuclease


entry: 3.1.31.1
reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
name:
--- 
- micrococcal nuclease
- spleen endonuclease
- thermonuclease
- nuclease T
- micrococcal endonuclease
- nuclease T'
- staphylococcal nuclease
- spleen phosphodiesterase
- Staphylococcus aureus nuclease
- Staphylococcus aureus nuclease B
- ribonucleate (deoxynucleate) 3'-nucleotidohydrolase

comment:
Hydrolyses double- or single-stranded substrate. Formerly EC 3.1.4.7. cf. EC 3.1.16.1 spleen exonuclease.


entry: 3.1.-.-
name: --- []
reaction:
D-glycero-D-manno-Heptose 1,7-bisphosphate + H2O <=> D-glycero-D-manno-Heptose 1-phosphate + Orthophosphate [RN:R05647]


entry: 3.2.1.1
name: --- - alpha-amylase - glycogenase - alpha amylase, alpha-amylase - endoamylase - Taka-amylase A
sysname: 1,4-alpha-D-glucan glucanohydrolase
iubmb_reaction: (other) R02108 R06209(G)
kegg_reaction: R02108 R06209(G)
comment:
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.

reaction:
Endohydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides containing three or more 1,4-alpha-linked D-glucose units


entry: 3.2.1.2
name: --- - beta-amylase - saccharogen amylase - glycogenase - beta amylase, beta-amylase
sysname: 1,4-alpha-D-glucan maltohydrolase
iubmb_reaction: (other) R02112 R06159(G)
kegg_reaction: R02112 R06159(G)
comment:
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. The term 'beta' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.

reaction:
Hydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains


entry: 3.2.1.3
sysname: 1,4-alpha-D-glucan glucohydrolase
iubmb_reaction: (other) R01790 R01791 R06199(G)
kegg_reaction: R01790 R01791 R06199(G)
name:
--- 
- glucan 1,4-alpha-glucosidase
- glucoamylase
- amyloglucosidase
- gamma-amylase
- lysosomal alpha-glucosidase
- acid maltase
- exo-1,4-alpha-glucosidase
- glucose amylase
- gamma-1,4-glucan glucohydrolase

comment:
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.

reaction:
Hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose


entry: 3.2.1.4
sysname: 1,4-(1,3-1,4)-beta-D-glucan 4-glucanohydrolase
comment: Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
iubmb_reaction: (other) R02886 R06200(G)
kegg_reaction: R02886 R06200(G)
name:
--- 
- cellulase
- endo-1,4-beta-D-glucanase
- beta-1,4-glucanase
- beta-1,4-endoglucan hydrolase
- celluase A
- cellulosin AP
- endoglucanase D
- alkali cellulase
- cellulase A 3
- celludextrinase
- 9.5 cellulase
- avicelase
- pancellase SS


entry: 3.2.1.6
sysname: 1,3-(1,3-1,4)-beta-D-glucan 3(4)-glucanohydrolase
name:
--- 
- endo-1,3(4)-beta-glucanase
- endo-1,3-beta-D-glucanase
- laminarinase
- laminaranase
- beta-1,3-glucanase
- beta-1,3-1,4-glucanase
- endo-1,3-beta-glucanase
- endo-beta-1,3(4)-glucanase
- endo-beta-1,3-1,4-glucanase
- endo-beta-(1->3)-D-glucanase
- endo-1,3-1,4-beta-D-glucanase
- endo-beta-(1-3)-D-glucanase
- endo-beta-1,3-glucanase IV

comment:
Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 beta-N-acetylhexosaminidase.

reaction:
Endohydrolysis of 1,3- or 1,4-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3


entry: 3.2.1.8
sysname: 1,4-beta-D-xylan xylanohydrolase
reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans
name:
--- 
- endo-1,4-beta-xylanase
- endo-(1->4)-beta-xylanase(1->4)-beta-xylan 4-xylanohydrolase
- endo-1,4-xylanase
- xylanase
- beta-1,4-xylanase
- endo-beta-1,4-xylanase
- endo-1,4-beta-D-xylanase
- 1,4-beta-xylan xylanohydrolase
- beta-xylanase
- beta-1,4-xylan xylanohydrolase
- beta-D-xylanase


entry: 3.2.1.10
sysname: oligosaccharide alpha-1,6-glucohydrolase
iubmb_reaction: (other) R01718 R01791 R06080(G) R06199(G)
kegg_reaction: R01718 R01791 R06080(G) R06199(G)
name:
--- 
- oligo-1,6-glucosidase
- limit dextrinase (erroneous)
- isomaltase
- sucrase-isomaltase
- exo-oligo-1,6-glucosidase
- dextrin 6alpha-glucanohydrolase
- alpha-limit dextrinase
- dextrin 6-glucanohydrolase

comment:
This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.

reaction:
Hydrolysis of 1,6-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose


entry: 3.2.1.11
sysname: 1,6-alpha-D-glucan 6-glucanohydrolase
reaction: Endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran
name:
--- 
- dextranase
- dextran hydrolase
- endodextranase
- dextranase DL 2
- DL 2
- endo-dextranase
- alpha-D-1,6-glucan-6-glucanohydrolase


entry: 3.2.1.12
name: --- - Deleted entry
comment:
Deleted entry: cycloheptaglucanase. Now included with EC 3.2.1.54 cyclomaltodextrinase (EC 3.2.1.12 created 1961, deleted 1976)


entry: 3.2.1.13
name: --- - Deleted entry
comment:
Deleted entry: cyclohexaglucanase. Now included with EC 3.2.1.54 cyclomaltodextrinase (EC 3.2.1.13 created 1961, deleted 1976)


entry: 3.2.1.14
sysname: poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase
comment: Some chitinases also display the activity defined in EC 3.2.1.17 lysozyme.
reaction: Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins
iubmb_reaction: (other) R01206 R02334 R06081(G) R06082(G)
kegg_reaction: R01206 R02334 R06081(G) R06082(G)
name:
--- 
- chitinase
- chitodextrinase
- 1,4-beta-poly-N-acetylglucosaminidase
- poly-beta-glucosaminidase
- beta-1,4-poly-N-acetyl glucosamidinase


entry: 3.2.1.15
sysname: poly(1,4-alpha-D-galacturonide) glycanohydrolase
reaction: Random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans
iubmb_reaction: (other) R01982 R02360 R06201(G) R06239(G)
kegg_reaction: R01982 R02360 R06201(G) R06239(G)
name:
--- 
- polygalacturonase
- pectin depolymerase
- pectinase
- endopolygalacturonase
- pectolase
- pectin hydrolase
- pectin polygalacturonase
- endo-polygalacturonase
- poly-alpha-1,4-galacturonide glycanohydrolase
- endogalacturonase
- endo-D-galacturonase


entry: 3.2.1.17
sysname: peptidoglycan N-acetylmuramoylhydrolase
comment: cf. also EC 3.2.1.14 chitinase.
name:
--- 
- lysozyme
- muramidase
- globulin G
- mucopeptide glucohydrolase
- globulin G1
- N,O-diacetylmuramidase
- lysozyme g
- L-7001
- 1,4-N-acetylmuramidase
- mucopeptide N-acetylmuramoylhydrolase
- PR1-lysozyme

reaction:
Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins


entry: 3.2.1.18
name: --- - exo-alpha-sialidase - neuraminidase - sialidase - alpha-neuraminidase - acetylneuraminidase
sysname: acetylneuraminyl hydrolase
comment:
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.

reaction:
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates

iubmb_reaction:
(other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G)

kegg_reaction:
R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G)


entry: 3.2.1.20
sysname: alpha-D-glucoside glucohydrolase
iubmb_reaction: (other) R00028 R00801 R00802 R01101 R06084(G) R06087(G) R06088(G) R06091(G)
kegg_reaction: R00028 R00801 R00802 R01101 R06084(G) R06087(G) R06088(G) R06091(G)
name:
--- 
- alpha-glucosidase
- maltase
- glucoinvertase
- glucosidosucrase
- maltase-glucoamylase
- alpha-glucopyranosidase
- glucosidoinvertase
- alpha-D-glucosidase
- alpha-glucoside hydrolase
- alpha-1,4-glucosidase

comment:
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses 1,6-alpha-D-glucose links.

reaction:
Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose


entry: 3.2.1.21
sysname: beta-D-glucoside glucohydrolase
reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose
iubmb_reaction: (other) R00026 R02887 R03527 R04949 R04998 R06077(G) R06092(G)
kegg_reaction: R00026 R02887 R03527 R04949 R04998 R06077(G) R06092(G)
name:
--- 
- beta-glucosidase
- gentiobiase
- cellobiase
- emulsin
- elaterase
- aryl-beta-glucosidase
- beta-D-glucosidase
- beta-glucoside glucohydrolase
- arbutinase
- amygdalinase
- p-nitrophenyl beta-glucosidase
- primeverosidase
- amygdalase
- limarase
- salicilinase
- beta-1,6-glucosidase

comment:
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.


entry: 3.2.1.22
sysname: alpha-D-galactoside galactohydrolase
comment: Also hydrolyses alpha-D-fucosides.
name:
--- 
- alpha-galactosidase
- melibiase
- alpha-D-galactosidase
- alpha-galactosidase A
- alpha-galactoside galactohydrolase

reaction:
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase

iubmb_reaction:
(other) R01101 R01103 R01104 R01194 R01329 R02926 R03618 R03634 R04019 R04470 R05549 R05961(G) R06002(G) R06070(G) R06091(G) R06093(G) R06094(G) R06096(G) R06142(G) R06152(G)

kegg_reaction:
R01101 R01103 R01104 R01194 R01329 R02926 R03618 R03634 R04019 R04470 R05549 R05961(G) R06002(G) R06070(G) R06091(G) R06093(G) R06094(G) R06096(G) R06142(G) R06152(G)


entry: 3.2.1.23
sysname: beta-D-galactoside galactohydrolase
reaction: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
name:
--- 
- beta-galactosidase
- lactase
- beta-lactosidase
- maxilact
- hydrolact
- beta-D-lactosidase
- S 2107
- lactozym
- trilactase
- beta-D-galactanase
- oryzatym
- sumiklat

comment:
Some enzymes in this group hydrolyse alpha-L-arabinosides; some animal enzymes also hydrolyse beta-D-fucosides and beta-D-glucosides; cf. EC 3.2.1.108 lactase.

iubmb_reaction:
(other) R01105 R01678 R01679 R03355 R03616 R04633 R04783 R05112 R05994(G) R06010(G) R06098(G) R06099(G) R06111(G) R06144(G) R06202(G)

kegg_reaction:
R01105 R01678 R01679 R03355 R03616 R04633 R04783 R05112 R05994(G) R06010(G) R06098(G) R06099(G) R06111(G) R06144(G) R06202(G)


entry: 3.2.1.24
sysname: alpha-D-mannoside mannohydrolase
reaction: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
name:
--- 
- alpha-mannosidase
- alpha-D-mannosidase
- p-nitrophenyl-alpha-mannosidase
- alpha-D-mannopyranosidase
- 1,2-alpha-mannosidase
- 1,2-alpha-D-mannosidase
- exo-alpha-mannosidase

comment:
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.


entry: 3.2.1.25
sysname: beta-D-mannoside mannohydrolase
reaction: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides
name:
--- 
- beta-mannosidase
- mannanase
- mannase
- beta-D-mannosidase
- beta-mannoside mannohydrolase
- exo-beta-D-mannanase


entry: 3.2.1.26
sysname: beta-D-fructofuranoside fructohydrolase
comment: Substrates include sucrose; also catalyses fructotransferase reactions.
reaction: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
iubmb_reaction: (other) R00802 R02410 R03635 R03921 R06088(G) R06100(G) R06101(G) R06102(G)
kegg_reaction: R00802 R02410 R03635 R03921 R06088(G) R06100(G) R06101(G) R06102(G)
name:
--- 
- beta-fructofuranosidase
- invertase
- saccharase
- glucosucrase
- beta-h-fructosidase
- beta-fructosidase
- invertin
- sucrase
- maxinvert L 1000
- fructosylinvertase
- alkaline invertase
- acid invertase


entry: 3.2.1.29
name: --- - Deleted entry
comment:
Deleted entry: chitobiase. Now included with EC 3.2.1.52 beta-L-N-acetylhexosaminidase (EC 3.2.1.29 created 1961, deleted 1972)


entry: 3.2.1.30
name: --- - Deleted entry
comment:
Deleted entry: beta-D-acetylglucosaminidase. Now included with EC 3.2.1.52 beta-L-N-acetylhexosaminidase (EC 3.2.1.30 created 1961, deleted 1992)


entry: 3.2.1.31
sysname: beta-D-glucuronoside glucuronosohydrolase
reaction: a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol [RN:R01478]
iubmb_reaction: R01478
kegg_reaction: R04979
name:
--- 
- beta-glucuronidase
- beta-glucuronide glucuronohydrolase glucuronidase
- exo-beta-D-glucuronidase
- ketodase


entry: 3.2.1.32
sysname: 1,3-beta-D-xylan xylanohydrolase
reaction: Random hydrolysis of 1,3-beta-D-glycosidic linkages in 1,3-beta-D-xylans
name:
--- 
- xylan endo-1,3-beta-xylosidase
- xylanase
- endo-1,3-beta-xylanase
- endo-1,3-xylanase
- 1,3-beta-xylanase
- 1,3-xylanase
- beta-1,3-xylanase
- endo-beta-1,3-xylanase


entry: 3.2.1.33
sysname: glycogen phosphorylase-limit dextrin alpha-1,6-glucohydrolase
reaction: Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
iubmb_reaction: (other) R02109 R06158(G)
kegg_reaction: R02109 R06158(G)
name:
--- 
- amylo-alpha-1,6-glucosidase
- amylo-1,6-glucosidase
- dextrin 6-alpha-D-glucosidase
- amylopectin 1,6-glucosidase
- dextrin-1,6-glucosidase

comment:
This enzyme hydrolyses an unsubstituted (1->6)-alpha-glucose residue that forms a branch point on an alpha-(1->4)-linked glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-alpha-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system.


entry: 3.2.1.34
name: --- - Deleted entry
comment:
Deleted entry: chondroitinase. Now included with EC 3.2.1.35 hyalurononglucosaminidase (EC 3.2.1.34 created 1965, deleted 1972)


entry: 3.2.1.35
sysname: hyaluronate 4-glycanohydrolase
name:
--- 
- hyaluronoglucosaminidase
- hyaluronidase
- hyaluronoglucosidase
- chondroitinase
- chondroitinase I

comment:
Also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.

reaction:
Random hydrolysis of 1->4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate


entry: 3.2.1.36
sysname: hyaluronate 3-glycanohydrolase
name:
--- 
- hyaluronoglucuronidase
- hyaluronidase
- glucuronoglucosaminoglycan hyaluronate lyase
- orgelase

reaction:
Random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate


entry: 3.2.1.37
sysname: 1,4-beta-D-xylan xylohydrolase
iubmb_reaction: (other) R01433 R06203(G)
kegg_reaction: R01433 R06203(G)
name:
--- 
- xylan 1,4-beta-xylosidase
- xylobiase
- beta-xylosidase
- exo-1,4-beta-xylosidase
- beta-D-xylopyranosidase
- exo-1,4-xylosidase
- exo-1,4-beta-D-xylosidase

comment:
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.

reaction:
Hydrolysis of 1,4-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini


entry: 3.2.1.38
name: --- - beta-D-fucosidase - beta-fucosidase
sysname: beta-D-fucoside fucohydrolase
reaction: Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides
comment:
Enzymes from some sources also hydrolyse beta-D-galactosides and/or beta-D-glucosides and/or alpha-L-arabinosides. The activity of EC 3.2.1.37 xylan 1,4-beta-xylosidase, is an associated activity found in some sources (e.g. liver)


entry: 3.2.1.39
sysname: 1,3-beta-D-glucan glucanohydrolase
reaction: Hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans
iubmb_reaction: (other) R00308 R06204(G)
kegg_reaction: R00308 R06204(G)
name:
--- 
- glucan endo-1,3-beta-D-glucosidase
- endo-1,3-beta-glucanase
- laminarinase
- laminaranase
- oligo-1,3-glucosidase
- callase
- beta-1,3-glucanase
- kitalase
- 1,3-beta-D-glucan 3-glucanohydrolase
- endo-(1,3)-beta-D-glucanase
- (1->3)-beta-glucan endohydrolase
- endo-(1->3)-beta-D-glucanase
- (1->3)-beta-glucan 3-glucanohydrolase
- endo-1,3-beta-D-glucanase
- endo-1,3-beta-glucosidase

comment:
Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. Hydrolyses laminarin, paramylon and pachyman.


entry: 3.2.1.41
sysname: pullulan alpha-1,6-glucanohydrolase
name:
--- 
- pullulanase
- limit dextrinase (erroneous)
- amylopectin 6-glucanohydrolase
- bacterial debranching enzyme
- debranching enzyme
- alpha-dextrin endo-1,6-alpha-glucosidase
- R-enzyme

comment:
Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an alpha-(1->6)-linkage.

reaction:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan [a linear polymer of alpha-(1->6)-linked maltotriose units] and in amylopectin and glycogen, and the alpha- and beta-limit dextrins of amylopectin and glycogen


entry: 3.2.1.42
sysname: GDP-glucose glucohydrolase
reaction: GDP-glucose + H2O = D-glucose + GDP [RN:R00337]
iubmb_reaction: R00337
name:
--- 
- GDP-glucosidase
- guanosine diphosphoglucosidase
- guanosine diphosphate D-glucose glucohydrolase


entry: 3.2.1.45
sysname: D-glucosyl-N-acylsphingosine glucohydrolase
comment: Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
reaction: D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine [RN:R01498]
iubmb_reaction: R01498
name:
--- 
- glucosylceramidase
- psychosine hydrolase
- glucosphingosine glucosylhydrolase
- GlcCer-beta-glucosidase
- beta-D-glucocerebrosidase
- glucosylcerebrosidase
- beta-glucosylceramidase
- ceramide glucosidase
- glucocerebrosidase
- glucosylsphingosine beta-glucosidase
- glucosylsphingosine beta-D-glucosidase


entry: 3.2.1.46
sysname: D-galactosyl-N-acylsphingosine galactohydrolase
comment: cf. EC 3.2.1.62 glycosylceramidase.
reaction: D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine [RN:R01502]
iubmb_reaction: R01502 > R03617
name:
--- 
- galactosylceramidase
- cerebroside galactosidase
- galactocerebroside.beta-galactosidase
- galactosylcerebrosidase
- galactocerebrosidase
- ceramide galactosidase
- galactocerebroside galactosidase
- galactosylceramide.beta-galactosidase
- cerebroside beta-galactosidase
- galactosylceramidase I
- beta-galactosylceramidase
- galactocerebroside-beta-D-galactosidase
- lactosylceramidase I
- beta-galactocerebrosidase
- lactosylceramidase


entry: 3.2.1.47
sysname: D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine galactohydrolase
iubmb_reaction: R03487 R06136(G)
name:
--- 
- galactosylgalactosylglucosylceramidase
- trihexosyl ceramide galactosidase
- ceramide trihexosidase
- ceramidetrihexoside alpha-galactosidase
- trihexosylceramide alpha-galactosidase
- ceramidetrihexosidase

reaction:
D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H2O = D-galactose + lactosyl-N-acylsphingosine [RN:R03487 R06136]


entry: 3.2.1.48
sysname: sucrose-alpha-D-glucohydrolase
reaction: Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
iubmb_reaction: (other) R00802 R06088(G)
kegg_reaction: R00802 R06088(G)
name:
--- 
- sucrose alpha-glucosidase
- sucrose alpha-glucohydrolase
- sucrase
- sucrase-isomaltase
- sucrose.alpha.-glucohydrolase
- intestinal sucrase
- sucrase(invertase)

comment:
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).


entry: 3.2.1.49
sysname: alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
comment: Splits N-acetylgalactosaminyl groups from O-3 of Ser and Thr.
iubmb_reaction: (other) R04183 R05966(G)
kegg_reaction: R04183 R05966(G)
name:
--- 
- alpha-N-acetylgalactosaminidase
- alpha-acetylgalactosaminidase
- N-acetyl-alpha-D-galactosaminidase
- N-acetyl-alpha-galactosaminidase

reaction:
Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides


entry: 3.2.1.50
sysname: alpha-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase
comment: Hydrolyses UDP-N-acetylglucosamine.
name:
--- 
- alpha-N-acetylglucosaminidase
- alpha-acetylglucosaminidase
- N-acetyl-alpha-D-glucosaminidase
- N-acetyl-alpha-glucosaminidase
- alpha-D-2-acetamido-2-deoxyglucosidase

reaction:
Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides


entry: 3.2.1.52
sysname: beta-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase
comment: Acts on N-acetylglucosides and N-acetylgalactosides.
reaction: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
iubmb_reaction: (other) R00022 R03492 R04184 R04586 R05963(G) R06001(G) R06004(G) R06141(G)
kegg_reaction: R00022 R03492 R04184 R04586 R05963(G) R06001(G) R06004(G) R06141(G)
name:
--- 
- beta-N-acetylhexosaminidase
- hexosaminidase
- beta-acetylaminodeoxyhexosidase
- N-acetyl-beta-D-hexosaminidase
- N-acetyl-beta-hexosaminidase
- beta-hexosaminidase
- beta-acetylhexosaminidinase
- beta-D-N-acetylhexosaminidase
- beta-N-acetyl-D-hexosaminidase
- beta-N-acetylglucosaminidase
- hexosaminidase A
- N-acetylhexosaminidase
- beta-D-hexosaminidase


entry: 3.2.1.53
sysname: beta-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
name:
--- 
- beta-N-acetylgalactosaminidase
- N-acetyl-beta-galactosaminidase
- N-acetyl-beta-D-galactosaminidase
- beta-acetylgalactosaminidase
- beta-D-N-acetylgalactosaminidase
- N-acetylgalactosaminidase

reaction:
Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides


entry: 3.2.1.55
sysname: alpha-L-arabinofuranoside arabinofuranohydrolase
reaction: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
iubmb_reaction: (other) R01762 R06205(G)
kegg_reaction: R01762 R06205(G)
name:
--- 
- alpha-N-arabinofuranosidase
- arabinosidase
- alpha-arabinosidase
- alpha-L-arabinosidase
- alpha-arabinofuranosidase
- polysaccharide alpha-L-arabinofuranosidase
- alpha-L-arabinofuranoside hydrolase
- L-arabinosidase
- alpha-L-arabinanase

comment:
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides.


entry: 3.2.1.56
name: --- - glucuronosyl-disulfoglucosamine glucuronidase - glycuronidase
sysname: 3-D-glucuronsyl-N2,6-disulfo-beta-D-glucosamine glucuronohydrolase
iubmb_reaction: R04512 R06143(G)
reaction:
3-D-glucuronosyl-N2,6-disulfo-beta-D-glucosamine + H2O = D-glucuronate + N2,6-disulfo-D-glucosamine [RN:R04512 R06143]


entry: 3.2.1.57
name: --- - isopullulanase
sysname: pullulan 4-glucanohydrolase (isopanose-forming)
reaction: Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose)
comment:
The enzyme has practically no action on starch. Panose (4-alpha-isomaltosylglucose) is hydrolysed to isomaltose and glucose. cf. EC 3.2.1.41 (pullulanase) and EC 3.2.1.135 (neopullulanase).


entry: 3.2.1.58
sysname: 1,3-beta-glucan glucohydrolase
comment: Acts on oligosaccharides, but very slowly on laminaribiose.
iubmb_reaction: (other) R03115 R06078(G)
kegg_reaction: R03115 R06078(G)
name:
--- 
- glucan 1,3-beta-glucosidase
- exo-1,3-beta-glucosidase
- beta-1,3-glucan exo-hydrolase
- exo (1->3)-beta-glucanase
- exo-beta-1,3-glucanase
- exo-1,3-beta-glucanase
- exo-beta-(1->3)-D-glucanase
- exo-beta-1,3-D-glucanase
- exo-1,3-beta-D-glucanase
- exo-beta-(1->3)-glucanohydrolase

reaction:
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing alpha-glucose


entry: 3.2.1.59
sysname: 1,3(1,3-1,4)-alpha-D-glucan 3-glucanohydrolase
comment: Products from pseudonigeran (1,3-alpha-D-glucan) are nigerose and alpha-D-glucose.
reaction: Endohydrolysis of 1,3-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran
name:
--- 
- glucan endo-1,3-alpha-glucosidase
- endo-1,3-alpha-glucanase
- mutanase
- endo-(1->3)-alpha-glucanase
- cariogenase
- cariogenanase
- endo-1,3-alpha-D-glucanase


entry: 3.2.1.60
name: --- - glucan 1,4-alpha-maltotetraohydrolase - exo-maltotetraohydrolase
sysname: 1,4-alpha-D-glucan maltotetraohydrolase
comment:
Compare EC 3.2.1.2 beta-amylase, which removes successive maltose residues, and EC 3.2.1.98 (glucan 1,4-alpha-maltohexaosidase) and EC 3.2.1.116 (glucan 1,4-alpha-maltotriohydrolase).

reaction:
Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends


entry: 3.2.1.61
name: --- - mycodextranase
sysname: 1,3-1,4-alpha-D-glucan 4-glucanohydrolase
comment:
Products are nigerose and 4-alpha-D-nigerosylglucose. No hydrolysis of alpha-D-glucans containing only 1,3- or 1,4-bonds.

reaction:
Endohydrolysis of 1,4-alpha-D-glucosidic linkages in alpha-D-glucans containing both 1,3- and 1,4-bonds


entry: 3.2.1.62
sysname: glycosyl-N-acylsphingosine glycohydrolase
reaction: glycosyl-N-acylsphingosine + H2O = N-acylsphingosine + a sugar [RN:R01501]
iubmb_reaction: R01501
name:
--- 
- glycosylceramidase
- phlorizin hydrolase
- phloretin-glucosidase
- glycosyl ceramide glycosylhydrolase
- cerebrosidase
- phloridzin beta-glucosidase
- lactase-phlorizin hydrolase
- phloridzin glucosidase

comment:
Broad specificity [cf. EC 3.2.1.45 (glucosylceramidase) and EC 3.2.1.46 (galactosylceramidase)]. Also hydrolyses phlorizin to phloretin and glucose. The intestinal enzyme is a complex that also catalyses the reaction of EC 3.2.1.108 lactase.


entry: 3.2.1.63
name: --- - 1,2-alpha-L-fucosidase - almond emulsin fucosidase - alpha-(1->2)-L-fucosidase
sysname: 2-alpha-L-fucopyranosyl-beta-D-galactoside fucohydrolase
iubmb_reaction: R04270 R06118(G)
comment:
Highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by a 1,2-alpha-linkage. Not identical with EC 3.2.1.111 1,3-alpha-L-fucosidase.

reaction:
methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O = L-fucose + methyl beta-D-galactoside [RN:R04270 R06118]


entry: 3.2.1.64
sysname: 2,6-beta-D-fructofuranan 6-(beta-D-fructosyl)-D-fructose-hydrolase
name:
--- 
- 2,6-beta-fructan 6-levanbiohydrolase
- beta-2,6-fructan-6-levanbiohydrolase
- 2,6-beta-D-fructan 6-levanbiohydrolase
- levanbiose-producing levanase
- 2,6-beta-D-fructan 6-beta-D-fructofuranosylfructohydrolase

reaction:
Hydrolysis of 2,6-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain


entry: 3.2.1.65
name: --- - levanase - levan hydrolase
sysname: 2,6-beta-D-fructan fructanohydrolase
iubmb_reaction: (other) R05624 R06206(G)
kegg_reaction: R05624 R06206(G)
reaction:
Random hydrolysis of 2,6-beta-D-fructofuranosidic linkages in 2,6-beta-D-fructans (levans) containing more than 3 fructose units


entry: 3.2.1.67
sysname: poly(1,4-alpha-D-galacturonide) galacturonohydrolase
iubmb_reaction: R04320 R06201(G)
kegg_reaction: R01982 R07413
name:
--- 
- galacturan 1,4-alpha-galacturonidase
- exopolygalacturonase
- poly(galacturonate) hydrolase
- exo-D-galacturonase
- exo-D-galacturonanase
- exopoly-D-galacturonase

reaction:
(1,4-alpha-D-galacturonide)n + H2O = (1,4-alpha-D-galacturonide)(n-1) + D-galacturonate [RN:R04320 R06201]


entry: 3.2.1.68
name: --- - isoamylase - debranching enzyme
sysname: glycogen alpha-1,6-glucanohydrolase
comment:
Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41 (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability to hydrolyse pullulan, and by limited action on alpha-limit dextrins. Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage.

reaction:
Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins


entry: 3.2.1.69
name: --- - Deleted entry
comment:
Deleted entry: amylopectin 6-glucanohydrolase. Now included with EC 3.2.1.41 pullulanase (EC 3.2.1.69 created 1972, deleted 1976)


entry: 3.2.1.70
name: --- - glucan 1,6-alpha-glucosidase - exo-1,6-beta-glucosidase - glucodextrinase
sysname: glucan alpha-1,6-D-glucohydrolase
comment:
Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the beta-configuration. Dextrans and isomaltosaccharides are hydrolysed, as is isomaltose, but very slowly. The enzyme from some sources also possesses the activity of EC 3.2.1.59 (glucan endo-1,3-alpha-glucosidase).

reaction:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D-glucans and derived oligosaccharides


entry: 3.2.1.71
sysname: 1,2-beta-D-glucan glucanohydrolase
reaction: Random hydrolysis of 1,2-glucosidic linkages in 1,2-beta-D-glucans
name:
--- 
- glucan endo-1,2-beta-glucosidase
- endo-1,2-beta-glucanase
- beta-D-1,2-glucanase
- endo-(1->2)-beta-D-glucanase


entry: 3.2.1.72
sysname: 1,3-beta-D-xylan xylohydrolase
reaction: Hydrolysis of successive xylose residues from the non-reducing termini of 1,3-beta-D-xylans
name:
--- 
- xylan 1,3-beta-xylosidase
- 1,3-beta-D-xylosidase, exo-1,3-beta-xylosidase
- beta-1,3'-xylanase
- exo-beta-1,3'-xylanase


entry: 3.2.1.73
sysname: 1,3-1,4-beta-D-glucan 4-glucanohydrolase
reaction: Hydrolysis of 1,4-beta-D-glucosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds
name:
--- 
- licheninase
- lichenase
- beta-(1->3), (1->4)-D-glucan 4-glucanohydrolase
- 1,3-1,4-beta-glucan endohydrolase
- 1,3-1,4-beta-glucan 4-glucanohydrolase

comment:
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.


entry: 3.2.1.74
sysname: 1,4-beta-D-glucan glucohydrolase
comment: Acts on 1,4-beta-D-glucans and related oligosaccharides. Cellobiose is hydrolysed, but very slowly.
reaction: Hydrolysis of 1,4-linkages in 1,4-beta-D-glucans, to remove successive glucose units
name:
--- 
- glucan 1,4-beta-glucosidase
- exo-1,4-beta-glucosidase
- exocellulase
- exo-beta-1,4-glucosidase
- exo-beta-1,4-glucanase
- beta-1,4-beta-glucanase
- beta-glucosidase
- exo-1,4-beta-glucanase

iubmb_reaction:
(other) R00306 R01444 R03801 R03802 R05141 R05142 R06104(G) R06105(G) R06106(G) R06107(G) R06108(G) R06109(G)

kegg_reaction:
R00306 R01444 R03801 R03802 R05141 R05142 R06104(G) R06105(G) R06106(G) R06107(G) R06108(G) R06109(G)


entry: 3.2.1.75
sysname: 1,6-beta-D-glucan glucanohydrolase
comment: Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
reaction: Random hydrolysis of 1,6-linkages in 1,6-beta-D-glucans
name:
--- 
- glucan endo-1,6-beta-glucosidase
- endo-1,6-beta-glucanase
- beta-1->6-Glucan hydrolase
- endo-beta-1,6-glucanase
- endo-(1->6)-beta-D-glucanase
- beta-1,6-glucanase-pustulanase
- beta-1,6-glucan hydrolase
- beta-1,6-glucan 6-glucanohydrolase


entry: 3.2.1.77
name: --- - mannan 1,2-(1,3)-alpha-mannosidase - exo-1,2-1,3-alpha-mannosidase
sysname: 1,2-1,3-alpha-D-mannan mannohydrolase
reaction: Hydrolysis of 1,2- and 1,3-linkages in yeast mannan, releasing mannose
iubmb_reaction: (other) R01331(G) R05816 R06150(G) R06151(G)
kegg_reaction: R01331(G) R05816 R06150(G) R06151(G)
comment:
A 1,6-alpha-D-mannan backbone remains after action on yeast mannan. This is further attacked, but slowly.


entry: 3.2.1.78
sysname: 1,4-beta-D-mannan mannanohydrolase
reaction: Random hydrolysis of 1,4-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans
iubmb_reaction: (other) R01332 R06207(G)
kegg_reaction: R01332 R06207(G)
name:
--- 
- mannan endo-1,4-beta-mannosidase
- endo-1,4-beta-mannanase
- endo-beta-1,4-mannase
- beta-mannanase B
- beta-1, 4-mannan 4-mannanohydrolase
- endo-beta-mannanase
- beta-D-mannanase


entry: 3.2.1.79
name: --- - Deleted entry
comment:
Deleted entry: alpha-L-arabinofuranoside hydrolase. Now included with EC 3.2.1.55 alpha-N-arabinofuranosidase (EC 3.2.1.79 created 1972, deleted 1976)


entry: 3.2.1.80
sysname: beta-D-fructan fructohydrolase
comment: Hydrolyses inulin and levan, and also sucrose.
reaction: Hydrolysis of terminal, non-reducing 2,1- and 2,6-linked beta-D-fructofuranose residues in fructans
iubmb_reaction: (other) R00879 R06208(G)
kegg_reaction: R00879 R06208(G)
name:
--- 
- fructan beta-fructosidase
- exo-beta-D-fructosidase
- exo-beta-fructosidase
- polysaccharide beta-fructofuranosidase
- fructan exohydrolase


entry: 3.2.1.81
sysname: agarose 4-glycanohydrolase
name:
--- 
- beta-agarase
- agarase (ambiguous)
- AgaA
- AgaB
- endo-beta-agarase
- agarose 3-glycanohydrolase (incorrect)

comment:
Also acts on porphyran, but more slowly [1]. This enzyme cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place [6]. The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB [6].

reaction:
Hydrolysis of 1,4-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product


entry: 3.2.1.83
name: --- - kappa-carrageenase - kappa-carrageenan 4-beta-D-glycanohydrolase
sysname: kappa-carrageenan 4-beta-D-glycanohydrolase (configuration-retaining)
comment:
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157 (iota-carrageenase), but similar to EC 3.2.1.81 (beta-agarase), this enzyme proceeds with retention of the anomeric configuration.

reaction:
Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans


entry: 3.2.1.85
sysname: 6-phospho-beta-D-galactoside 6-phosphogalactohydrolase
reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol [RN:R03255]
iubmb_reaction: R03255 > R03256 R06110(G)
name:
--- 
- 6-phospho-beta-galactosidase
- phospho-beta-galactosidase
- beta-D-phosphogalactoside galactohydrolase
- phospho-beta-D-galactosidase
- 6-phospho-beta-D-galactosidase


entry: 3.2.1.86
sysname: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose glucohydrolase
comment: Also hydrolyses several other phospho-beta-D-glucosides, but not their non-phosphorylated forms.
iubmb_reaction: R00839 R06112(G)
kegg_reaction: R05133 R05134
name:
--- 
- 6-phospho-beta-glucosidase
- phospho-beta-glucosidase A
- phospho-beta-glucosidase
- phosphocellobiase

reaction:
6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate [RN:R00839 R06112]


entry: 3.2.1.87
sysname: Aerobacter-capsular-polysaccharide galactohydrolase
name:
--- 
- capsular-polysaccharide endo-1,3-alpha-galactosidase
- polysaccharide depolymerase
- capsular polysaccharide galactohydrolase

comment:
Hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.

reaction:
Random hydrolysis of 1,3-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide


entry: 3.2.1.89
sysname: arabinogalactan 4-beta-D-galactanohydrolase
reaction: Endohydrolysis of 1,4-beta-D-galactosidic linkages in arabinogalactans
name:
--- 
- arabinogalactan endo-1,4-beta-galactosidase
- endo-1,4-beta-galactanase
- galactanase
- arabinogalactanase


entry: 3.2.1.90
name: --- - Deleted entry
comment:
Deleted entry: arabinogalactan endo-1,3-beta-galactosidase not sufficiently characterised. (EC 3.2.1.90 created 1976, deleted 2001)


entry: 3.2.1.91
sysname: 1,4-beta-D-glucan cellobiohydrolase
iubmb_reaction: (other) R02886 R06200(G)
kegg_reaction: R02886 R06200(G)
name:
--- 
- cellulose 1,4-beta-cellobiosidase
- exo-cellobiohydrolase
- beta-1,4-glucan cellobiohydrolase
- beta-1,4-glucan cellobiosylhydrolase
- 1,4-beta-glucan cellobiosidase
- exoglucanase
- avicelase
- CBH 1
- C1 cellulase
- cellobiohydrolase I
- cellobiohydrolase
- exo-beta-1,4-glucan cellobiohydrolase
- 1,4-beta-D-glucan cellobiohydrolase
- cellobiosidase

reaction:
Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains


entry: 3.2.1.92
sysname: peptidoglycan beta-N-acetylmuramoylexohydrolase
reaction: Hydrolysis of terminal, non-reducing N-acetylmuramic residues
name:
--- 
- peptidoglycan beta-N-acetylmuramidase
- exo-beta-N-acetylmuramidase
- exo-beta-acetylmuramidase
- beta-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside acetamidodeoxyglucohydrolase


entry: 3.2.1.94
sysname: 1,6-alpha-D-glucan isomaltohydrolase
name:
--- 
- glucan 1,6-alpha-isomaltosidase
- exo-isomaltohydrolase
- isomalto-dextranase
- isomaltodextranase
- G2-dextranase

comment:
Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolysed at slower rates.

reaction:
Hydrolysis of 1,6-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains


entry: 3.2.1.95
name: --- - dextran 1,6-alpha-isomaltotriosidase - exo-isomaltotriohydrolase
sysname: 1,6-alpha-D-glucan isomaltotriohydrolase
reaction:
Hydrolysis of 1,6-alpha-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains


entry: 3.2.1.96
comment: A group of related enzymes.
name:
--- 
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- N,N'-diacetylchitobiosyl beta-N-acetylglucosaminidase
- endo-beta-N-acetylglucosaminidase
- mannosyl-glycoprotein endo-beta-N-acetylglucosamidase
- di-N-acetylchitobiosyl beta-N-acetylglucosaminidase
- endo-beta-acetylglucosaminidase
- endo-beta-(1->4)-N-acetylglucosaminidase
- mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase
- endoglycosidase S
- endo-N-acetyl-beta-D-glucosaminidase
- endo-N-acetyl-beta-glucosaminidase
- endo-beta-N-acetylglucosaminidase D
- endo-beta-N-acetylglucosaminidase F
- endo-beta-N-acetylglucosaminidase H
- endo-beta-N-acetylglucosaminidase L

sysname:
glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase

reaction:
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact


entry: 3.2.1.97
sysname: D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
comment: The aglycone may be serine or threonine.
name:
--- 
- glycopeptide alpha-N-acetylgalactosaminidase
- endo-alpha-N-acetylgalactosaminidase
- endo-alpha-acetylgalactosaminidase

reaction:
Hydrolysis of terminal D-galactosyl-N-acetyl-alpha-D-galactosaminidic residues from a variety of glycopeptides and glycoproteins


entry: 3.2.1.98
name: --- - glucan 1,4-alpha-maltohexaosidase - exo-maltohexaohydrolase
sysname: 1,4-alpha-D-glucan maltohexaohydrolase
comment:
cf. EC 3.2.1.3 glucan 1,4-alpha-glucosidase, which removes successive glucose residues; EC 3.2.1.2 beta-amylase, which removes successive maltose residues; EC 3.2.1.116 glucan 1,4-alpha-maltotriohydrolase, which removes successive maltotriose units and EC 3.2.1.60 glucan 1,4-alpha-maltotetraohydrolase, which removes successive maltotetraose residues. The products have the alpha-configuration.

reaction:
Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends


entry: 3.2.1.99
sysname: 1,5-alpha-L-arabinan 1,5-alpha-L-arabinanohydrolase
comment: Also acts on beet arabinan, but more slowly.
reaction: Endohydrolysis of 1,5-alpha-arabinofuranosidic linkages in 1,5-arabinans
name:
--- 
- arabinan endo-1,5-alpha-L-arabinosidase
- endo-1,5-alpha-L-arabinanase
- endo-alpha-1,5-arabanase
- endo-arabanase


entry: 3.2.1.100
sysname: 1,4-beta-D-mannan mannobiohydrolase
name:
--- 
- mannan 1,4-mannobiosidase
- 1,4-beta-D-mannan mannobiohydrolase
- exo-beta-mannanase
- exo-1,4-beta-mannobiohydrolase

reaction:
Hydrolysis of 1,4-beta-D-mannosidic linkages in 1,4-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends


entry: 3.2.1.101
sysname: 1,6-alpha-D-mannan mannanohydrolase
reaction: Random hydrolysis of 1,6-alpha-D-mannosidic linkages in unbranched 1,6-mannans
name:
--- 
- mannan endo-1,6-alpha-mannosidase
- exo-1,6-beta-mannanase
- endo-alpha-1->6-D-mannanase
- endo-1,6-beta-mannanase
- mannan endo-1,6-beta-mannosidase


entry: 3.2.1.102
name: --- - blood-group-substance endo-1,4-beta-galactosidase - endo-beta-galactosidase
sysname: blood-group-substance 1,4-beta-D-galactanohydrolase
reaction: Endohydrolysis of 1,4-beta-D-galactosidic linkages in blood group A and B substances
comment:
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to a 1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-alpha-D-fucosyl residue.


entry: 3.2.1.103
sysname: keratan-sulfate 1,4-beta-D-galactanohydrolase
reaction: Endohydrolysis of 1,4-beta-D-galactosidic linkages in keratan sulfate
name:
--- 
- keratan-sulfate endo-1,4-beta-galactosidase
- endo-beta-galactosidase
- keratan sulfate endogalactosidase
- keratanase

comment:
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-alpha-D-N-acetyl-glucosaminyl residues. Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102 blood-group-substance endo-1,4-beta-galactosidase).


entry: 3.2.1.104
name: --- - steryl-beta-glucosidase
sysname: cholesteryl-beta-D-glucoside glucohydrolase
reaction: cholesteryl-beta-D-glucoside + H2O = D-glucose + cholesterol [RN:R01460]
iubmb_reaction: R01460
comment:
Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol.


entry: 3.2.1.105
name: --- - 3alpha(S)-strictosidine beta-glucosidase
sysname: strictosidine beta-D-glucohydrolase
reaction: strictosidine + H2O = D-glucose + strictosidine aglycone [RN:R03820]
iubmb_reaction: R03820
comment:
Does not act on a number of closely related glycosides. Strictosidine is a precursor of indole alkaloids.


entry: 3.2.1.106
sysname: mannosyl-oligosaccharide glucohydrolase
iubmb_reaction: (other) R05979(G)
kegg_reaction: R05979(G)
name:
--- 
- mannosyl-oligosaccharide glucosidase
- Glc3Man9NAc2 oligosaccharide glucosidase
- trimming glucosidase I

comment:
Also acts, more slowly, on the corresponding glycolipids and glycopeptides. Involved in the formation of high-mannose and complex glycoproteins.

reaction:
Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc3Man9GlcNAc2


entry: 3.2.1.107
sysname: protein-alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine glucohydrolase
comment: Requires free, positively charged epsilon-amino group of hydroxylysine.
iubmb_reaction: R04503
name:
--- 
- protein-glucosylgalactosylhydroxylysine glucosidase
- 2-O-alpha-D-glucopyranosyl-5-O-alpha-D-galactopyranosylhydroxy-L- lysine glucohydrolase

reaction:
protein alpha-D-glucosyl-1,2-beta-D-galactosyl-L-hydroxylysine + H2O = D-glucose + protein beta-D-galactosyl-L-hydroxylysine [RN:R04503]


entry: 3.2.1.108
name: --- - lactase - lactase-phlorizin hydrolase
sysname: lactose galactohydrolase
reaction: lactose + H2O = D-galactose + D-glucose [RN:R01100 R06114]
iubmb_reaction: R01100 R06114(G) > R01678 R06098(G)
comment:
The enzyme from intestinal mucosa is isolated as a complex that also catalyses the reaction of EC 3.2.1.62 glycosylceramidase. cf. EC 3.2.1.33 amylo-alpha-1,6-glucosidase.


entry: 3.2.1.110
sysname: D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine mucinaminohydrolase
iubmb_reaction: R04527 R06140(G)
name:
--- 
- mucinaminylserine mucinaminidase
- endo-alpha-N-acetylgalactosaminidase
- endo-alpha-N-acetyl-D-galactosaminidase

reaction:
D-galactosyl-3-(N-acetyl-beta-D-galactosaminyl)-L-serine + H2O = D-galactosyl-3-N-acetyl-beta-D-galactosamine + L-serine [RN:R04527 R06140]


entry: 3.2.1.113
sysname: 1,2-alpha-mannosyl-oligosaccharide alpha-D-mannohydrolase
comment: Involved in the synthesis of glycoproteins.
iubmb_reaction: (other) R05982(G) R06722(G)
kegg_reaction: R05982(G) R06722(G)
name:
--- 
- mannosyl-oligosaccharide 1,2-alpha-mannosidase
- mannosidase 1A
- mannosidase 1B
- 1,2-alpha-mannosidase
- exo-alpha-1,2-mannanase
- mannose-9 processing alpha-mannosidase
- glycoprotein processing mannosidase I
- mannosidase I
- Man9-mannosidase

reaction:
Hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2


entry: 3.2.1.114
sysname: 1,3-(1,6-)mannosyl-oligosaccharide alpha-D-mannohydrolase
comment: Involved in the synthesis of glycoproteins.
iubmb_reaction: (other) R05984(G)
kegg_reaction: R05984(G)
name:
--- 
- mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
- mannosidase II
- exo-1,3-1,6-alpha-mannosidase
- alpha-D-mannosidase II
- alpha-mannosidase II
- alpha1-3,6-mannosidase
- GlcNAc transferase I-dependent alpha1,3[alpha1,6]mannosidase
- Golgi alpha-mannosidase II

reaction:
Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3


entry: 3.2.1.115
sysname: 1,2-alpha-D-glucosyl-branched-dextran 2-glucohydrolase
name:
--- 
- branched-dextran exo-1,2-alpha-glucosidase
- dextran 1,2-alpha-glucosidase
- dextran alpha-1,2 debranching enzyme

comment:
Does not hydrolyse disaccharides or oligosaccharides containing linear 1,2-alpha-glucosidic linkages.

reaction:
Hydrolysis of 1,2-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose


entry: 3.2.1.116
name: --- - glucan 1,4-alpha-maltotriohydrolase - exo-maltotriohydrolase - maltotriohydrolase
sysname: 1,4-alpha-D-glucan maltotriohydrolase
comment:
cf. EC 3.2.1.2 (beta-amylase), EC 3.2.1.60 (glucan 1,4-alpha-maltotetraohydrolase) and EC 3.2.1.98 (glucan 1,4-alpha-maltohexaosidase). The products have the alpha-configuration.

reaction:
Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends


entry: 3.2.1.117
sysname: amygdalin beta-D-glucohydrolase
reaction: (R)-amygdalin + H2O = (R)-prunasin + D-glucose [RN:R02985]
iubmb_reaction: R02985
name:
--- 
- amygdalin beta-glucosidase
- amygdalase
- amygdalinase
- amygdalin hydrolase
- amygdalin glucosidase

comment:
Highly specific; does not act on prunasin, linamarin, gentiobiose or cellobiose (cf. EC 3.2.1.21 beta-glucosidase).


entry: 3.2.1.118
name: --- - prunasin beta-glucosidase - prunasin hydrolase
sysname: prunasin beta-D-glucohydrolase
reaction: (R)-prunasin + H2O = D-glucose + mandelonitrile [RN:R02558]
iubmb_reaction: R02558
comment:
Highly specific; does not act on amygdalin, linamarin or gentiobiose. (cf. EC 3.2.1.21 beta-glucosidase).


entry: 3.2.1.119
name: --- - vicianin beta-glucosidase - vicianin hydrolase
sysname: (R)-vicianin beta-D-glucohydrolase
reaction: (R)-vicianin + H2O = mandelonitrile + vicianose [RN:R03642]
iubmb_reaction: R03642
comment:
Also hydrolyses, more slowly, (R)-amygdalin and (R)-prunasin, but not gentiobiose, linamarin or cellobiose.


entry: 3.2.1.120
sysname: oligoxyloglucan xyloglucohydrolase
name:
--- 
- oligoxyloglucan beta-glycosidase
- isoprimeverose-producing oligoxyloglucan hydrolase
- oligoxyloglucan hydrolase

reaction:
Hydrolysis of 1,4-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose (i.e. alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing chain ends


entry: 3.2.1.122
name: --- - maltose-6'-phosphate glucosidase - phospho-alpha-glucosidase
sysname: maltose-6'-phosphate 6-phosphoglucohydrolase
reaction: maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate [RN:R00838 R06115]
iubmb_reaction: R00838 R06115(G)
kegg_reaction: R00837 R06113(G)
comment:
Hydrolyses a variety of 6-phospho-D-glucosides, including maltose 6-phosphate, alpha,alpha-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by Fe(II), Mn(II), Co(II) and Ni(II). It is rapidly inactivated in air.


entry: 3.2.1.123
sysname: oligoglycosylglucosylceramide glycohydrolase
reaction: oligoglycosylglucosylceramide + H2O = ceramide + oligoglycosylglucose [RN:R04118 R06157]
iubmb_reaction: R04118 R06157(G)
kegg_reaction: R06283(G)
name:
--- 
- endoglycosylceramidase
- endoglycoceramidase
- EGCase
- glycosyl-N-acetyl-sphingosine 1,1-beta-D-glucanohydrolase

comment:
An enzyme from Rhodococcus sp. that degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond. Does not act on monoglycosylceramides. cf. EC 3.2.1.62 glycosylceramidase.


entry: 3.2.1.124
sysname: capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase
name:
--- 
- 3-deoxy-2-octulosonidase
- 2-keto-3-deoxyoctonate hydrolase
- octulosylono hydrolase
- octulofuranosylono hydrolase
- octulopyranosylonohydrolase

comment:
The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.

reaction:
Endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides


entry: 3.2.1.125
sysname: raucaffricine beta-D-glucohydrolase
comment: Highly specific; some other ajmalan glucoside alkaloids are hydrolysed, but more slowly.
reaction: raucaffricine + H2O = D-glucose + vomilenine [RN:R03703]
iubmb_reaction: R03703
name:
--- 
- raucaffricine beta-glucosidase
- raucaffricine beta-D-glucosidase
- raucaffricine glucosidase


entry: 3.2.1.126
name: --- - coniferin beta-glucosidase - coniferin-hydrolyzing beta-glucosidase
sysname: coniferin beta-D-glucosidase
reaction: coniferin + H2O = D-glucose + coniferol [RN:R02595]
iubmb_reaction: R02595
kegg_reaction: R03604 R04006
comment:
Also hydrolyses syringin, 4-cinnamyl alcohol beta-glucoside and, more slowly, some other aryl beta-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.


entry: 3.2.1.127
name: --- - 1,6-alpha-L-fucosidase - alpha-L-fucosidase
sysname: 1,6-L-fucosyl-N-acetyl-D-glucosaminylglycopeptide fucohydrolase
comment: The enzyme from Aspergillus niger does not act on 1,2-, 1,3-, or 1,4-L-fucosyl linkages.
reaction:
Hydrolysis of 1,6-linkages between alpha-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin


entry: 3.2.1.128
sysname: glycyrrhizinate glucuronosylhydrolase
reaction: glycyrrhizinate + H2O = 1,2-beta-D-glucuronosyl-D-glucuronate + glycyrrhetinate [RN:R03906]
iubmb_reaction: R03906
name:
--- 
- glycyrrhizinate beta-glucuronidase
- glycyrrhizin beta-hydrolase
- glycyrrhizin hydrolase
- glycyrrhizinic acid hydrolase

comment:
The enzyme from Aspergillus niger is specific for the hydrolysis of the triterpenoid glycoside glycyrrhizinate from roots of Glycyrrhiza sp.


entry: 3.2.1.129
sysname: polysialoside (2->8)-alpha-sialosylhydrolase
reaction: Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids
name:
--- 
- endo-alpha-sialidase
- endo-N-acylneuraminidase
- endoneuraminidase
- endo-N-acetylneuraminidase
- poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase
- poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase
- endosialidase
- endo-N

comment:
Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetylated substrates. An exo-alpha-sialidase activity is listed as EC 3.2.1.18 exo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.


entry: 3.2.1.130
sysname: glycoprotein glucosylmannohydrolase
comment: Involved in the synthesis of glycoproteins.
name:
--- 
- glycoprotein endo-alpha-1,2-mannosidase
- glucosylmannosidase
- endo-alpha-D-mannosidase
- endo-alpha-mannosidase
- endomannosidase
- glucosyl mannosidase

reaction:
Hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of the glycoprotein produced in the Golgi membrane


entry: 3.2.1.132
name: --- - chitosanase
sysname: chitosan N-acetylglucosaminohydrolase
reaction: Endohydrolysis of beta-1,4-linkages between D-glucosamine residues in a partly acetylated chitosan
iubmb_reaction: (other) R02833 R06175(G)
kegg_reaction: R02833 R06175(G)
comment:
A whole spectrum of chitosanases are now known (for more details, see http://callisto.si.usherb.ca/~rbrzezin/index.html). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.


entry: 3.2.1.133
name: --- - glucan 1,4-alpha-maltohydrolase - maltogenic alpha-amylase
sysname: 1,4-alpha-D-glucan alpha-maltohydrolase
comment:
Acts on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.

reaction:
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains


entry: 3.2.1.134
name: --- - difructose-anhydride synthase - inulobiose hydrolase
sysname: bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase
reaction: bis-D-fructose 2',1:2,1'-dianhydride + H2O = inulobiose [RN:R03685 R06161]
iubmb_reaction: R03685 R06161(G)
comment:
Produces difructose anhydride by the reverse reaction of partial hydrolysis, forming an alpha-fructosidic linkage.


entry: 3.2.1.136
sysname: glucuronoarabinoxylan 1,4-beta-D-xylanohydrolase
comment: High activity towards feruloylated arabinoxylans from cereal plant cell walls.
reaction: Endohydrolysis of 1,4-beta-D-xylosyl links in some glucuronoarabinoxylans
name:
--- 
- glucuronoarabinoxylan endo-1,4-beta-xylanase
- feraxan endoxylanase
- feraxanase
- endoarabinoxylanase
- glucuronoxylan xylohydrolase
- glucuronoxylanase
- glucuronoxylan xylanohydrolase


entry: 3.2.1.139
name: --- - alpha-glucuronidase - alpha-glucosiduronase
sysname: alpha-D-glucosiduronate glucuronohydrolase
reaction: an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate [RN:R01480]
iubmb_reaction: R01480
comment:
considerable differences in the specificities of the enzymes from different fungi for alpha-D-glucosiduronates have been reported. Activity is also found in the snail.


entry: 3.2.1.140
name: --- - lacto-N-biosidase
sysname: oligosaccharide lacto-N-biosylhydrolase
iubmb_reaction: (other) R05166 R06116(G)
kegg_reaction: R05166 R06116(G)
comment:
the enzyme from Streptomyces specifically hydrolyses the terminal lacto-N-biosyl residue (beta-D-Gal-(1->3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->R). Lacto-N-hexaose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-beta-D-Glc NAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolysed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. Asialo GM1 tetraose (beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolysed very slowly, but lacto-N-neotetraose (beta-D-Gal-(1->4)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is not a substrate

reaction:
(1) beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H2O = beta-D-Gal-(1->3)-D-GlcNAc + beta-D-Gal-(1->4)-D-Glc; (2) lacto-N-tetraose + H2O = lacto-N-biose + lactose


entry: 3.2.1.141
sysname: 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose glucanohydrolase (trehalose-producing)
name:
--- 
- 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase
- malto-oligosyltrehalose trehalohydrolase

reaction:
hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-{(1->4)-alpha-D-glucanosyl}n trehalose to yield trehalose and alpha-(1->4)-D-glucan


entry: 3.2.1.142
name: --- - limit dextrinase - R-enzyme - amylopectin-1,6-glucosidase
sysname: dextrin alpha-1,6-glucanohydrolase
comment:
Plant enzymes with little or no action on glycogen. Action on amylopectin is incomplete, but action on alpha-limit dextrins is complete. Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage.

reaction:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan


entry: 3.2.1.143
name: --- - poly(ADP-ribose) glycohydrolase
comment: Specific to (1"-2') linkage of ribose-ribose bond of poly(ADP-ribose).
reaction:
hydrolyses poly(ADP-ribose) at glycosidic (1"-2') linkage of ribose-ribose bond to produce free ADP-ribose


entry: 3.2.1.144
name: --- - 3-deoxyoctulosonase - alpha-Kdo-ase
sysname: 3-deoxyoctulosonyl-lipopolysaccharide hydrolase
iubmb_reaction: R06054
comment:
Releases Kdo (alpha- and beta-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is also a substrate.

reaction:
3-deoxyoctulosonyl-lipopolysaccharide+ H2O = 3-deoxyoctulosonic acid + lipopolysaccharide [RN:R06054]


entry: 3.2.1.145
name: --- - galactan 1,3-beta-galactosidase
sysname: galactan (1->3)-beta-D-galactosidase
reaction: Hydrolysis of terminal, non-reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans
comment:
This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (1->6)-beta-D-galactobiose, and galactose bearing oligosaccharide chains on O-6. Hence, it releases branches from [arabino-galacto-(1->6)]-(1->3)-beta-D-galactans.


entry: 3.2.1.146
sysname: beta-D-galactofuranoside hydrolase
reaction: Hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose
name:
--- 
- beta-galactofuranosidase
- exo-beta-galactofuranosidase
- exo-beta-D-galactofuranosidase
- beta-D-galactofuranosidase

comment:
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.


entry: 3.2.1.148
name: --- - Deleted entry
comment:
Deleted entry: ribosylhomocysteinase. The activity is most probably attributable to EC 4.4.1.21 S-ribosylhomocysteine lyase (EC 3.2.1.148 created 1972 as EC 3.3.1.3, transferred 2001 to EC 3.2.1.148, transferred 2004 to EC 3.13.1.2, deleted 2005)


entry: 3.2.1.149
name: --- - beta-primeverosidase
sysname: 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside 6-O-(beta-D-xylosyl)-beta-D-glucohydrolase
iubmb_reaction: R05788
comment:
The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to beta-primeverosides [i.e. 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranosides], it also hydrolyses 6-O-(beta-D-apiofuranosyl)-beta-D-glucopyranosides and, less rapidly, beta-vicianosides and 6-O-(alpha-L-arabinofuranosyl)-beta-D-glucopyranosides, but not beta-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed.

reaction:
a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H2O = 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol [RN:R05788]


entry: 3.2.1.150
name: --- - oligoxyloglucan reducing-end-specific cellobiohydrolase
sysname: oligoxyloglucan reducing-end cellobiohydrolase
comment:
The enzyme is found in the fungus Geotrichum sp. M128. The substrate is a hemicellulose found in plant cell walls.

reaction:
Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-1,4-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.


entry: 3.2.1.151
sysname: [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase
name:
--- 
- xyloglucan-specific endo-beta-1,4-glucanase
- XEG
- xyloglucan endo-beta-1,4-glucanase
- xyloglucanase
- xyloglucanendohydrolase
- XH
- 1,4-beta-D-glucan glucanohydrolase

comment:
The enzyme for Aspergillus aculeatus is specific for xyloglucan and does not hydrolyse other cell-wall components. It cleaves glycosidic bonds with retention of the beta-configuration of the glycosyl residues.

reaction:
xyloglucan + H2O = xyloglucan oligosaccharides (endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan)


entry: 3.2.1.152
name: --- - mannosylglycoprotein endo-beta-mannosidase - endo-beta-mannosidase
comment:
The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the beta-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum.

reaction:
Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-beta-D-N- acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequences


entry: 3.2.1.153
sysname: beta-(2,1)-D-fructan fructohydrolase
reaction: Hydrolysis of terminal, non-reducing 2,1-linked beta-D-fructofuranose residues in fructans
name:
--- 
- fructan beta-(2,1)-fructosidase
- beta-(2-1)-D-fructan fructohydrolase
- beta-(2-1)fructan exohydrolase
- inulinase
- 1-FEH II
- 1-fructan exohydrolase
- 1-FEH w1
- 1-FEH w2
- beta-(2-1)-linkage-specific fructan-beta-fructosidase

comment:
Possesses one of the activities of EC 3.2.1.80, fructan beta-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 1,1-nystose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-beta-D- fructofuranosyl alpha-D-glucopyranoside), some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan beta-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.


entry: 3.2.1.154
name: --- - fructan beta-(2,6)-fructosidase - beta-(2-6)-fructan exohydrolase - levanase - 6-FEH
sysname: beta-(2,6)-D-fructan fructohydrolase
reaction: Hydrolysis of terminal, non-reducing 2,6-linked beta-D-fructofuranose residues in fructans
comment:
Possesses one of the activities of EC 3.2.1.80, fructan beta-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 6,6-kestotetraose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl-(2->6)-beta-D- fructofuranosyl alpha-D-glucopyranoside), some (but not all) inulin-type fructans can also be hydrolysed, but more slowly (cf. EC 3.2.1.153, fructan beta-(2,1)-fructosidase). Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.


entry: 3.2.1.155
name: --- - xyloglucan-specific exo-beta-1,4-glucanase - Cel74A
sysname: [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucanohydrolase
comment:
The enzyme from the fungus Chrysosporium lucknowense is an endoglucanase when it acts on linear substrates without bulky substituents on the polymeric backbone (e.g. carboxymethylcellulose), but switches to an exoglucanase mode of action when bulky side chains are present (as in the case of xyloglucan). The enzyme can also act on barley beta-glucan, but more slowly.

reaction:
xyloglucan + H2O = xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan)


entry: 3.2.1.156
sysname: beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylop yranose reducing-end xylanase
reaction: Hydrolysis of 1,4-beta-D-xylose residues from the reducing end of oligosaccharides
name:
--- 
- oligosaccharide reducing-end xylanase
- Rex
- reducing end xylose-releasing exo-oligoxylanase

comment:
The enzyme acts rapidly on the beta-anomer of beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylop yranose, leaving the new reducing end in the alpha configuration. It also acts on longer oligosaccharides that have this structure at their reducing ends. The penultimate residue must be xylose, but replacing either of the other two residues with glucose merely slows the rate greatly.


entry: 3.2.1.157
name: --- - iota-carrageenase
sysname: iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting)
comment:
The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate. iota-Neocarraoctaose is the shortest substrate oligomer that can be cleaved. Unlike EC 3.2.1.81, beta-agarase and EC 3.2.1.83, kappa-carrageenase, this enzyme proceeds with inversion of the anomeric configuration. iota-Carrageenan differs from kappa-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the kappa-compound on O-4 of the D-galactose residues.

reaction:
Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans


entry: 3.2.1.158
name: --- - alpha-agarase - agarase (ambiguous) - agaraseA33
sysname: agarose 3-glycanohydrolase
comment:
Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. While the enzyme can also hydrolyse the highly sulfated agarose porphyran very efficiently, it cannot hydrolyse the related compounds kappa-carrageenan (see EC 3.2.1.83) and iota-carrageenan (see EC 3.2.1.157) [2]. See also EC 3.2.1.81, beta-agarase.

reaction:
Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product


entry: 3.2.1.159
sysname: alpha-neoagaro-oligosaccharide 3-glycohydrolase
name:
--- 
- alpha-neoagaro-oligosaccharide hydrolase
- alpha-neoagarooligosaccharide hydrolase
- alpha-NAOS hydrolase

comment:
When neoagarohexaose is used as a substrate, the oligosaccharide is cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose and agaropentaose, which is further hydrolysed to agarobiose and agarotriose. With neoagarotetraose as substrate, the products are predominantly agarotriose and 3,6-anhydro-L-galactose. In Vibrio sp. the actions of EC 3.2.1.81, beta-agarase and EC 3.2.1.159 can be used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose.

reaction:
Hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose


entry: 3.2.1.160
name: --- - Deleted entry
comment:
Deleted entry: xyloglucan-specific exo-beta-1,4-glucanase. The enzyme was shown to be identical to EC 3.2.1.155, xyloglucan-specific exo-beta-1,4-glucanase, during the public-review process so was withdrawn before being made official. (EC 3.2.1.160 created 2006, deleted 2006)


entry: 3.2.1.161
name:
--- 
- beta-apiosyl-beta-glucosidase
- isoflavonoid-7-O-beta[D-apiosyl-(1->6)-beta-D-glucoside] disaccharidase
- isoflavonoid 7-O-beta-apiosyl-glucoside beta-glucosidase
- furcatin hydrolase

sysname:
7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid beta-D-apiofuranosyl-(1->6)-D-glucohydrolase

comment:
The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs in glycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and 7-hydroxy-2',4',5',6-tetramethoxy-7-O-beta-D-apiofuranosyl-(1->6)-be ta-D-glucopyranoside (dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides [2]. Daidzin and genistin are also substrates.

reaction:
7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose


entry: 3.2.1.-
name: --- []
reaction:
(1) D-Glucosamine + D-Glucosaminide <=> D-Glucosaminide + H2O [RN:R01966 R06225]; (2) Pentosans + H2O <=> Pentosans + D-Xylose [RN:R04937]; (3) Pentosans + H2O <=> Pentosans + L-Arabinose [RN:R04938]; (4) D-Glucosamine + Chitosan(n) <=> Chitosan(n+1) + H2O [RN:R06225]


entry: 3.2.2.1
sysname: purine-nucleoside ribohydrolase
reaction: a purine nucleoside + H2O = D-ribose + a purine base [RN:R02341]
iubmb_reaction: R02341 > R01245 R01677 R01770 R02143
kegg_reaction: R01273
name:
--- 
- purine nucleosidase
- nucleosidase
- purine beta-ribosidase
- purine nucleoside hydrolase
- purine ribonucleosidase
- ribonucleoside hydrolase
- nucleoside hydrolase
- N-ribosyl purine ribohydrolase
- nucleosidase g
- N-D-ribosylpurine ribohydrolase
- inosine-adenosine-guanosine preferring nucleoside hydrolase
- purine-specific nucleoside N-ribohydrolase
- IAG-nucleoside hydrolase
- IAG-NH

comment:
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates [6].


entry: 3.2.2.5
sysname: NAD+ glycohydrolase
comment: This enzyme can also hydrolyse NADP+ to yield phospho-ADP-ribose and nicotinamide, but more slowly.
reaction: NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
iubmb_reaction: R00102
kegg_reaction: R00119
name:
--- 
- NAD+ nucleosidase
- NADase
- DPNase
- DPN hydrolase
- NAD hydrolase
- diphosphopyridine nucleosidase
- nicotinamide adenine dinucleotide nucleosidase
- NAD glycohydrolase
- NAD nucleosidase
- nicotinamide adenine dinucleotide glycohydrolase


entry: 3.2.2.6
sysname: NAD(P)+ glycohydrolase
comment: Also catalyses transfer of ADP-ribose(P) residues.
reaction: NAD(P)+ + H2O = ADP-ribose(P) + nicotinamide [RN:R00102 R00119]
iubmb_reaction: R00102 R00119
name:
--- 
- NAD(P)+ nucleosidase
- nicotinamide adenine dinucleotide (phosphate) nucleosidase
- triphosphopyridine nucleotidase
- NAD(P) nucleosidase
- NAD(P)ase
- nicotinamide adenine dinucleotide (phosphate) glycohydrolase


entry: 3.2.2.7
sysname: adenosine ribohydrolase
comment: Also acts on adenosine N-oxide.
reaction: adenosine + H2O = D-ribose + adenine [RN:R01245]
iubmb_reaction: R01245
name:
--- 
- adenosine nucleosidase
- adenosinase
- N-ribosyladenine ribohydrolase
- adenosine hydrolase
- ANase


entry: 3.2.2.8
sysname: pyrimidine-nucleoside ribohydrolase
reaction: a pyrimidine nucleoside + H2O = D-ribose + a pyrimidine base [RN:R02172]
iubmb_reaction: R02172 > R02137
kegg_reaction: R01245 R01677 R01770
name:
--- 
- ribosylpyrimidine nucleosidase
- N-ribosylpyrimidine nucleosidase
- pyrimidine nucleosidase
- N-ribosylpyrimidine ribohydrolase
- pyrimidine nucleoside hydrolase
- RihB
- YeiK
- nucleoside ribohydrolase

comment:
Also hydrolyses purine D-ribonucleosides, but more slowly. 2'-, 3'- and 5'-deoxynucleosides are not substrates [3].


entry: 3.2.2.9
sysname: S-adenosyl-L-homocysteine homocysteinylribohydrolase
reaction: S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine [RN:R00194]
iubmb_reaction: R00194
kegg_reaction: R01401
name:
--- 
- adenosylhomocysteine nucleosidase
- S-adenosylhomocysteine hydrolase (ambiguous)
- S-adenosylhomocysteine nucleosidase
- 5'-methyladenosine nucleosidase
- S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
- AdoHcy/MTA nucleosidase

comment:
Also acts on S-methyl-5'-thioadenosine to give adenine and S-methyl-5-thioribose (cf. EC 3.2.2.16, methylthioadenosine nucleosidase).


entry: 3.2.2.11
name: --- - beta-aspartyl-N-acetylglucosaminidase - beta-aspartylacetylglucosaminidase
sysname: 1-beta-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
iubmb_reaction: R01266
reaction:
1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine [RN:R01266]


entry: 3.2.2.14
sysname: nicotinamide-nucleotide phosphoribohydrolase
reaction: nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide [RN:R01270]
iubmb_reaction: R01270
name:
--- 
- NMN nucleosidase
- NMNase
- nicotinamide mononucleotide nucleosidase
- nicotinamide mononucleotidase
- NMN glycohydrolase
- NMNGhase


entry: 3.2.2.15
sysname: DNA-deoxyinosine deoxyribohydrolase
reaction: Hydrolyses DNA and polynucleotides, releasing free hypoxanthine
name:
--- 
- DNA-deoxyinosine glycosylase
- DNA(hypoxanthine) glycohydrolase
- deoxyribonucleic acid glycosylase
- hypoxanthine-DNA glycosylase


entry: 3.2.2.16
sysname: S-methyl-5'-thioadenosine adeninehyrolase
comment: Does not act on S-adenosylhomocysteine. cf. EC 3.2.2.9 adenosylhomocysteine nucleosidase.
reaction: S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine [RN:R01401]
iubmb_reaction: R01401
name:
--- 
- methylthioadenosine nucleosidase
- 5'-methylthioadenosine nucleosidase
- MTA nucleosidase
- MeSAdo nucleosidase
- methylthioadenosine methylthioribohydrolase


entry: 3.2.2.17
sysname: deoxy-D-ribocyclobutadipyrimidine polynucleotidodeoxyribohydrolase
name:
--- 
- deoxyribodipyrimidine endonucleosidase
- pyrimidine dimer DNA-glycosylase
- endonuclease V
- deoxyribonucleate pyrimidine dimer glycosidase
- pyrimidine dimer DNA glycosylase
- T4-induced UV endonuclease
- PD-DNA glycosylase

reaction:
Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue


entry: 3.2.2.18
name: --- - Deleted entry
comment:
Deleted entry: glycopeptide N-glycosidase. Now included with EC 3.5.1.52 N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.2.2.18 created 1984, deleted 1989)


entry: 3.2.2.19
sysname: protein-N(omega)-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
reaction: protein-N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + protein-L-arginine
iubmb_reaction: (other) R01886
kegg_reaction: R01886
name:
--- 
- "[protein ADP-ribosylarginine] hydrolase"
- ADP-ribose-L-arginine cleavage enzyme
- ADP-ribosylarginine hydrolase
- N(omega)-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase

comment:
The enzyme will remove ADP-ribose from arginine residues in ADP-ribosylated proteins. The enzyme can also catalyse the reaction N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine.


entry: 3.2.2.20
sysname: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine
name:
--- 
- DNA-3-methyladenine glycosylase I
- deoxyribonucleate 3-methyladenine glycosidase I
- 3-methyladenine DNA glycosylase I
- DNA-3-methyladenine glycosidase I

comment:
Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA-[protein]-cysteine S-methyltransferase).


entry: 3.2.2.21
sysname: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
name:
--- 
- DNA-3-methyladenine glycosylase II
- deoxyribonucleate 3-methyladenine glycosidase II
- 3-methyladenine DNA glycosylase II
- DNA-3-methyladenine glycosidase II
- AlkA

comment:
Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA-[protein]-cysteine S-methyltransferase).

reaction:
Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine


entry: 3.2.2.22
sysname: rRNA N-glycohydrolase
reaction: Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes
name:
--- 
- rRNA N-glycosylase
- ribosomal ribonucleate N-glycosidase
- nigrin b
- RNA N-glycosidase
- rRNA N-glycosidase
- ricin
- momorcochin-S
- Mirabilis antiviral protein
- gelonin
- saporins

comment:
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.


entry: 3.2.2.23
sysname: DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
name:
--- 
- DNA-formamidopyrimidine glycosylase
- Fapy-DNA glycosylase
- deoxyribonucleate glycosidase
- 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase
- 2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase
- formamidopyrimidine-DNA glycosylase
- DNA-formamidopyrimidine glycosidase
- Fpg protein

comment:
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.

reaction:
Hydrolysis of DNA containing ring-opened N7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine


entry: 3.2.2.24
sysname: ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
reaction: ADP-D-ribosyl-[dinitrogen reductase] = ADP-D-ribose + [dinitrogen reductase] [RN:R03446]
iubmb_reaction: R03446
name:
--- 
- ADP-ribosyl-[dinitrogen reductase] hydrolase
- azoferredoxin glycosidase
- azoferredoxin-activating enzymes
- dinitrogenase reductase-activating glycohydrolase
- ADP-ribosyl glycohydrolase

comment:
Together with EC 2.4.2.37 NAD+-dinitrogen-reductase ADP-D-ribosyltransferase, , this enzyme controls the level of activity of EC 1.18.6.1 nitrogenase.


entry: 3.3.1.1
sysname: S-adenosyl-L-homocysteine hydrolase
reaction: S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
iubmb_reaction: R00192
kegg_reaction: R04936
name:
--- 
- adenosylhomocysteinase
- S-adenosylhomocysteine synthase
- S-adenosylhomocysteine hydrolase
- adenosylhomocysteine hydrolase
- S-adenosylhomocysteinase
- SAHase
- AdoHcyase


entry: 3.3.1.2
sysname: S-adenosyl-L-methionine hydrolase
comment: Also hydrolyses methylmethionine sulfonium salt to dimethyl sulfide and homoserine.
reaction: S-adenosyl-L-methionine + H2O = L-homoserine + methylthioadenosine [RN:R00175]
iubmb_reaction: R00175
name:
--- 
- adenosylmethionine hydrolase
- S-adenosylmethionine cleaving enzyme
- methylmethionine-sulfonium-salt hydrolase
- adenosylmethionine lyase


entry: 3.3.2.1
sysname: isochorismate pyruvate-hydrolase
reaction: isochorismate + H2O = 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate [RN:R03037]
iubmb_reaction: R03037
name:
--- 
- isochorismatase
- 2,3-dihydro-2,3-dihydroxybenzoate synthase
- 2,3-dihydroxy-2,3-dihydrobenzoate synthase
- 2,3-dihydroxy-2,3-dihydrobenzoic synthase


entry: 3.3.2.2
name: --- - alkenylglycerophosphocholine hydrolase - lysoplasmalogenase
sysname: 1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
iubmb_reaction: R02745
reaction:
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine [RN:R02745]


entry: 3.3.2.3
name: --- - Transferred to 3.3.2.9 and 3.3.2.10
comment:
Transferred entry: epoxide hydrolase. Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10). (EC 3.3.2.3 created 1978, modified 1999, deleted 2006)


entry: 3.3.2.5
name: --- - alkenylglycerophosphoethanolamine hydrolase
sysname: 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine aldehydohydrolase
iubmb_reaction: R03415
reaction:
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = an aldehyde + sn-glycero-3-phosphoethanolamine [RN:R03415]


entry: 3.3.2.6
name: --- - leukotriene-A4 hydrolase - LTA4 hydrolase - LTA4H - leukotriene A4 hydrolase
sysname: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate hydrolase
iubmb_reaction: R03057
comment:
This is a bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities [4,6]. It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates [6] (see EC 3.4.11.6, aminopeptidase B). It also converts leukotriene A4 into leukotriene B4, unlike EC 3.2.2.10, soluble epoxide hydrolase, which converts leukotriene A4 into 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid [3,4]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol-5,6-oxide hydrolase) [3].

reaction:
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate [RN:R03057]


entry: 3.3.2.7
sysname: (5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoat e hydrolase
iubmb_reaction: R04609
kegg_reaction: R07036
name:
--- 
- hepoxilin-epoxide hydrolase
- hepoxilin epoxide hydrolase
- hepoxylin hydrolase
- hepoxilin A3 hydrolase

comment:
Converts hepoxilin A3 into trioxilin A3. Highly specific for the substrate, having only slight activity with other epoxides such as leukotriene A4 and styrene oxide [2]. Hepoxilin A3 is an hydroxy-epoxide derivative of arachidonic acid that is formed via the 12-lipoxygenase pathway [2]. It is probable that this enzyme plays a modulatory role in inflammation, vascular physiology, systemic glucose metabolism and neurological function [4]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].

reaction:
(5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14- trienoate + H2O = (5Z,9E,14Z)-(8xi,11xi,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate [RN:R04609]


entry: 3.3.2.8
name: --- - limonene-1,2-epoxide hydrolase - limonene oxide hydrolase
sysname: limonene-1,2-epoxide hydrolase
reaction: limonene-1,2-epoxide + H2O = limonene-1,2-diol [RN:R05784]
iubmb_reaction: R05784
comment:
Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. Enzyme hydrolyses several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. It differs from the previously described epoxide hydrolases [EC 3.3.2.4 (trans-epoxysuccinate hydrolase), EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase) and EC 3.3.2.10 (soluble epoxide hydrolase)] as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl dicarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.


entry: 3.3.2.9
sysname: cis-stilbene-oxide hydrolase
reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol
iubmb_reaction: (other) R07013 R07014 R07027 R07071 R07072 R07082
kegg_reaction: R07013 R07014 R07027 R07071 R07072 R07082
name:
--- 
- microsomal epoxide hydrolase
- epoxide hydratase (ambiguous)
- microsomal epoxide hydratase
- epoxide hydrase
- microsomal epoxide hydrase
- arene-oxide hydratase (ambiguous)
- benzo[a]pyrene-4,5-oxide hydratase
- benzo(a)pyrene-4,5-epoxide hydratase
- aryl epoxide hydrase (ambiguous)
- cis-epoxide hydrolase
- mEH

comment:
This is a key hepatic enzyme that is involved in the metabolism of numerous xenobiotics, such as 1,3-butadiene oxide, styrene oxide and the polycyclic aromatic hydrocarbon benzo[a]pyrene 4,5-oxide [5-7]. In a series of oxiranes with a lipophilic substituent of sufficient size (styrene oxides), monosubstituted as well as 1,1- and cis-1,2-disubstituted oxiranes serve as substrates or inhibitors of the enzyme. However, trans-1,2-disubstituted, tri-and tetra-substituted oxiranes are not substrates [9]. The reaction involves the formation of an hydroxyalkyl-enzyme intermediate [10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol-5,6-oxide hydrolase) [7].


entry: 3.3.2.10
sysname: epoxide hydrolase
reaction: an epoxide + H2O = a glycol [RN:R02822]
iubmb_reaction: R02822 > R05842 R07108 R07109 R07110 R07111
name:
--- 
- soluble epoxide hydrolase
- epoxide hydrase (ambiguous)
- epoxide hydratase (ambiguous)
- arene-oxide hydratase (ambiguous)
- aryl epoxide hydrase (ambiguous)
- trans-stilbene oxide hydrolase
- sEH
- cytosolic epoxide hydrolase

comment:
Catalyses the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism [7]. It is involved in the metabolism of arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic acid epoxides. The EETs, which are endogenous chemical mediators, act at the vascular, renal and cardiac levels to regulate blood pressure [4,5]. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate phosphatase [1,2]. Like EC 3.3.2.9, microsomal epoxide hydrolase, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate [4,6]. The enzyme can also use leukotriene A4, the substrate of EC 3.3.2.6, leukotriene-A4 hydrolase, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B4 as the product [9,10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [7].


entry: 3.3.2.11
name: --- - cholesterol-5,6-oxide hydrolase - cholesterol-epoxide hydrolase - ChEH
sysname: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol hydrolase
comment:
The enzyme appears to work equally well with either epoxide as substrate [3]. The product is a competitive inhibitor of the reaction. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [3].

reaction:
(1) 5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol; (2) 5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol


entry: 3.3.2.-
name: --- []
reaction:
(1) 5,6beta-Epoxy-5beta-cholestane <=> 5alpha-Cholestan-5,6beta-diol [RN:R04791]; (2) Cholesterol-5beta,6beta-epoxide + H2O <=> 3beta,5alpha,6beta-Cholestanetriol [RN:R04792]; (3) Cholesterol-5alpha,6beta-epoxide + H2O <=> 3beta,5alpha,6beta-Cholestanetriol [RN:R04793]; (4) 5,6beta-Epoxy-5alpha-cholestane <=> 5alpha-Cholestan-5,6beta-diol [RN:R04794]; (5) Phenanthrene-9,10-oxide + H2O <=> trans-9(S),10(S)-Dihydrodiolphenanthrene [RN:R05658]; (6) 5,6-Epoxytetraene + H2O <=> Lipoxin A4 [RN:R07031]; (7) 5,6-Epoxytetraene + H2O <=> Lipoxin B4 [RN:R07032]; (8) Hepoxilin B3 + H2O <=> Trioxilin B3 [RN:R07037]; (9) 12(13)-EpOME + H2O <=> 12,13-DHOME [RN:R07121]; (10) 9(10)-EpOME + H2O <=> 9,10-DHOME [RN:R07122]


entry: 3.4.11.1
name:
--- 
- leucyl aminopeptidase
- leucine aminopeptidase
- leucyl peptidase
- peptidase S
- cytosol aminopeptidase
- cathepsin III
- L-leucine aminopeptidase
- leucinaminopeptidase
- leucinamide aminopeptidase
- FTBL proteins
- proteinates FTBL
- aminopeptidase II
- aminopeptidase III
- aminopeptidase I

comment:
A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Formerly EC 3.4.1.1

reaction:
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low


entry: 3.4.11.2
iubmb_reaction: (other) R00899 R04951
kegg_reaction: R00899 R04951
name:
--- 
- membrane alanyl aminopeptidase
- microsomal aminopeptidase
- aminopeptidase M
- aminopeptidase N
- particle-bound aminopeptidase
- amino-oligopeptidase
- alanine aminopeptidase
- membrane aminopeptidase I
- pseudo leucine aminopeptidase
- alanyl aminopeptidase
- alanine-specific aminopeptidase
- cysteinylglycine dipeptidase
- cysteinylglycinase
- L-alanine aminopeptidase
- CD13

comment:
A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1. Formerly EC 3.4.1.2

reaction:
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide


entry: 3.4.11.3
comment: A zinc-containing sialoglycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family)
name:
--- 
- cystinyl aminopeptidase
- cystyl-aminopeptidase
- oxytocinase
- cystine aminopeptidase
- L-cystine aminopeptidase
- oxytocin peptidase
- vasopresssinase

reaction:
Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however [4]


entry: 3.4.11.4
comment: A zinc enzyme, widely distributed in mammalian tissues. Formerly EC 3.4.1.3
reaction: Release of the N-terminal residue from a tripeptide
iubmb_reaction: (other) R00494
kegg_reaction: R00494
name:
--- 
- tripeptide aminopeptidase
- tripeptidase
- aminotripeptidase
- aminoexotripeptidase
- lymphopeptidase
- imidoendopeptidase
- peptidase B
- alanine-phenylalanine-proline arylamidase
- peptidase T


entry: 3.4.11.5
reaction: Release of N-terminal proline from a peptide
iubmb_reaction: (other) R00135
kegg_reaction: R00135
name:
--- 
- prolyl aminopeptidase
- proline aminopeptidase
- Pro-X aminopeptidase
- cytosol aminopeptidase V
- proline iminopeptidase

comment:
A Mn2+-requiring enzyme present in the cytosol of mammalian and microbial cells. In contrast to the mammalian form, the bacterial form of the enzyme (type example of peptidase family S33) hydrolyses both polyproline and prolyl-2-naphthylamide. The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1, leucyl aminopeptidase."


entry: 3.4.11.6
name:
--- 
- aminopeptidase B
- arylamidase II
- arginine aminopeptidase
- arginyl aminopeptidase
- Cl--activated arginine aminopeptidase
- cytosol aminopeptidase IV
- L-arginine aminopeptidase

comment:
Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6, leukotriene-A4 hydrolase [5,6]. Potently inhibited by arphamenine B, and also inhibited by chelating agents, N-ethylmaleimide, arphamenine A, amastatin and bestatin. A zinc metallopeptidase in family family M1 (membrane alanyl aminopeptidase family) [4,5].

reaction:
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys


entry: 3.4.11.7
reaction: Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
name:
--- 
- glutamyl aminopeptidase
- aminopeptidase A
- aspartate aminopeptidase
- angiotensinase A
- glutamyl peptidase
- Ca2+-activated glutamate aminopeptidase
- membrane aminopeptidase II
- antigen BP-1/6C3 of mouse B lymphocytes
- L-aspartate aminopeptidase
- angiotensinase A2

comment:
Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family)


entry: 3.4.11.8
name: --- - Transferred to 3.4.19.3
comment:
Transferred entry: now EC 3.4.19.3 - pyroglutamyl-peptidase I (EC 3.4.11.8 created 1972, deleted 1981)


entry: 3.4.11.9
name:
--- 
- Xaa-Pro aminopeptidase
- proline aminopeptidase
- aminopeptidase P
- aminoacylproline aminopeptidase
- X-Pro aminopeptidase

comment:
A Mn2+-dependent, generally membrane-bound enzyme present in both mammalian and bacterial cells. In peptidase family M24 (methionyl aminopeptidase family)

reaction:
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide


entry: 3.4.11.10
name: --- - bacterial leucyl aminopeptidase - Aeromonas proteolytica aminopeptidase
reaction: Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
comment:
A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Staphylococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively)


entry: 3.4.11.13
name: --- - clostridial aminopeptidase - Clostridium histolyticum aminopeptidase
comment: A secreted enzyme from Clostridium histolyticum, requiring Mn2+ or Co2+
reaction:
Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-Pro-


entry: 3.4.11.14
name:
--- 
- cytosol alanyl aminopeptidase
- arylamidase
- aminopolypeptidase
- thiol-activated aminopeptidase
- human liver aminopeptidase
- puromycin-sensitive aminopeptidase
- soluble alanyl aminopeptidase
- cytosol aminopeptidase III
- alanine aminopeptidase

comment:
A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family)

reaction:
Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides


entry: 3.4.11.15
reaction: Preferentially, release of N-terminal lysine
name:
--- 
- aminopeptidase Y
- aminopeptidase Co
- aminopeptidase (cobalt-activated)
- lysyl aminopeptidase

comment:
Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more slowly, Arg-NHPhNO2. Type example of peptidase family M28


entry: 3.4.11.16
name: --- - Xaa-Trp aminopeptidase - aminopeptidase W - aminopeptidase X-Trp - X-Trp aminopeptidase
comment: A glycoprotein containing Zn2+, from renal and intestinal brush border membranes
reaction:
Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu-|-Trp, Leu-|-Trp and a number of other dipeptides


entry: 3.4.11.18
reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
name:
--- 
- methionyl aminopeptidase
- methionine aminopeptidase
- peptidase M
- L-methionine aminopeptidase
- MAP

comment:
Membrane-bound enzyme present in both prokaryotes and eukaryotes. Type example of peptidase family M24. Releases methionine from nascent peptides


entry: 3.4.11.19
name: --- - D-stereospecific aminopeptidase - D-aminopeptidase
comment:
Known from the bacterium Ochrobactrum anthropi. In peptidase family S12 (D-Ala-D-Ala carboxypeptidase family) [2]

reaction:
Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides and methyl esters also are hydrolysed, as is glycine amide


entry: 3.4.11.20
name: --- - aminopeptidase Ey
comment:
A zinc glycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family), composed of two 150 kDa subunits. From the plasma fraction of hen egg yolk

reaction:
Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position


entry: 3.4.11.21
name: --- - aspartyl aminopeptidase
reaction: Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
comment:
Aminoacyl-arylamides are poor substrates. This is an abundant cytosolic enzyme in mammalian cells, in peptidase family M18 of aminopeptidase I


entry: 3.4.11.22
name:
--- 
- aminopeptidase I
- aminopeptidase III
- aminopeptidase yscI
- leucine aminopeptidase IV
- yeast aminopeptidase I

comment:
A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18

reaction:
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates


entry: 3.4.11.23
name: --- - PepB aminopeptidase - Salmonella enterica serovar Typhimurium peptidase B
comment:
A 270-kDa protein composed of six 46.3-kDa subunits. The pH optimum is in the alkaline range and activity is stimulated by KCl. In peptidase family M17.

reaction:
Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln


entry: 3.4.13.1
name: --- - Transferred to 3.4.13.18
comment:
Transferred entry: now EC 3.4.13.18 - cytosol nonspecific dipeptidase (EC 3.4.13.1 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992])


entry: 3.4.13.2
name: --- - Transferred to 3.4.13.18
comment:
Transferred entry: now EC 3.4.13.18 - cytosol nonspecific dipeptidase (EC 3.4.13.2 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992])


entry: 3.4.13.3
reaction: Hydrolysis of Xaa-|-His dipeptides
iubmb_reaction: (other) R01166 R01992
kegg_reaction: R01166 R01992
name:
--- 
- X-His dipeptidase
- aminoacylhistidine dipeptidase
- carnosinase
- homocarnosinase
- dipeptidase M

comment:
A mammalian cytosolic enzyme that also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Activated by thiols; inhibited by metal-chelating agents. This enzyme in peptidase family M25 may be identical with cytosol nonspecific dipeptidase, EC 3.4.13.18. Formerly EC 3.4.3.3 and EC 3.4.13.13


entry: 3.4.13.4
comment: Widely distributed in mammals
reaction: Preferential hydrolysis of Xaa-|-Arg, Xaa-|-Lys or Xaa-|-ornithine dipeptides
iubmb_reaction: (other) R00911 R03935
kegg_reaction: R00911 R03935
name:
--- 
- Xaa-Arg dipeptidase
- aminoacyl-lysine dipeptidase
- N2-(4-amino-butyryl)-L-lysine hydrolase
- X-Arg dipeptidase


entry: 3.4.13.5
comment: Is identical with acetylhistidine deacetylase (formerly EC 3.5.1.34). Formerly EC 3.4.3.4
iubmb_reaction: (other) R03288
kegg_reaction: R03288
name:
--- 
- Xaa-methyl-His dipeptidase
- anserinase
- aminoacyl-methylhistidine dipeptidase
- acetylhistidine deacetylase
- N-acetylhistidine deacetylase
- alpha-N-acetyl-L-histidine aminohydrolase
- X-methyl-His dipeptidase

reaction:
Hydrolysis of anserine (beta-alanyl-|-N(pi)-methyl-L-histidine), carnosine, homocarnosine, glycyl-|-leucine and other dipeptides with broad specificity


entry: 3.4.13.6
name: --- - Transferred to 3.4.11.2
comment:
Transferred entry: now EC 3.4.11.2 - Membrane alanyl aminopeptidase (EC 3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC 3.4.13.6)


entry: 3.4.13.8
name: --- - Transferred to 3.4.13.18
comment:
Transferred entry: now EC 3.4.13.18 - cytosol nonspecific dipeptidase (EC 3.4.13.8 created 1961 as EC 3.4.3.6, transferred 1972 to EC 3.4.13.8)


entry: 3.4.13.9
name:
--- 
- Xaa-Pro dipeptidase
- prolidase
- imidodipeptidase
- proline dipeptidase
- peptidase D
- gamma-peptidase
- X-Pro dipeptidase

comment:
A Mn2+-activated enzyme, in peptidase family M24 (methionyl aminopeptidase family); cytosolic from most animal tissues. Formerly EC 3.4.3.7

reaction:
Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro


entry: 3.4.13.10
name: --- - Transferred to 3.4.19.5
comment:
Transferred entry: now EC 3.4.19.5 - beta-aspartyl-peptidase (EC 3.4.13.10 created 1972, deleted 1992)


entry: 3.4.13.11
name: --- - Transferred to 3.4.13.18 and 3.4.13.19
comment:
Transferred entry: now included in EC 3.4.13.18 - cytosol nonspecific dipeptidase, and EC 3.4.13.19 - membrane dipeptidase (EC 3.4.13.11 created 1972, deleted 1992)


entry: 3.4.13.13
name: --- - Transferred to 3.4.13.3
comment:
Transferred entry: now included with EC 3.4.13.3 - Xaa-His dipeptidase (EC 3.4.13.13 created 1981, deleted 1992)


entry: 3.4.13.15
name: --- - Transferred to 3.4.13.18
comment:
Transferred entry: now included with EC 3.4.13.18 - cytosol nonspecific dipeptidase (EC 3.4.13.15 created 1989, deleted 1992)


entry: 3.4.13.17
comment: A digestive enzyme of cephalopods
reaction: Hydrolysis of dipeptides containing either D- or L-amino acids or both
name:
--- 
- non-stereospecific dipeptidase
- peptidyl-D-amino acid hydrolase
- D-(or L-)aminoacyl-dipeptidase


entry: 3.4.13.18
reaction: Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids
name:
--- 
- cytosol nonspecific dipeptidase
- N2-beta-alanylarginine dipeptidase
- glycyl-glycine dipeptidase
- glycyl-leucine dipeptidase
- iminodipeptidase
- peptidase A
- Pro-X dipeptidase
- prolinase
- prolyl dipeptidase
- prolylglycine dipeptidase
- L-prolylglycine dipeptidase
- diglycinase
- Gly-Leu hydrolase
- glycyl-L-leucine dipeptidase
- glycyl-L-leucine hydrolase
- glycyl-L-leucine peptidase
- L-amino-acyl-L-amino-acid hydrolase
- glycylleucine peptidase
- glycylleucine hydrolase
- glycylleucine dipeptide hydrolase
- non-specific dipeptidase
- human cytosolic non-specific dipeptidase

comment:
A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine. Formerly EC 3.4.3.1, EC 3.4.3.2, EC 3.4.3.6, EC 3.4.13.1, EC 3.4.13.2, EC 3.4.13.8, EC 3.4.13.11 and EC 3.4.13.15


entry: 3.4.13.19
reaction: Hydrolysis of dipeptides
name:
--- 
- membrane dipeptidase
- renal dipeptidase
- dehydropeptidase I (DPH I)
- dipeptidase
- aminodipeptidase
- dipeptide hydrolase
- dipeptidyl hydrolase
- nonspecific dipeptidase
- glycosyl-phosphatidylinositol-anchored renal dipeptidase
- MDP

comment:
A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19. Formerly EC 3.4.13.11


entry: 3.4.13.20
name: --- - beta-Ala-His dipeptidase - serum carnosinase
iubmb_reaction: (other) R01166 R03286
kegg_reaction: R01166 R03286
comment:
Present in the serum of humans and higher primates, but not in the serum of other mammals. Activated by Cd2+ and citrate. Belongs in peptidase family M20.

reaction:
Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine


entry: 3.4.13.21
name:
--- 
- dipeptidase E
- aspartyl dipeptidase
- peptidase E
- PepE gene product (Salmonella typhimurium)

comment:
A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more slowly than dipeptides with free C-termini. No peptide larger than a C-blocked dipeptide is known to be a substrate. Asp-NH-Np is hydrolysed and is a convenient substrate for routine assay. The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. Belongs in peptidase family S51.

reaction:
Dipeptidase E catalyses the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides


entry: 3.4.13.22
reaction: D-Ala-D-Ala + H2O = 2 D-Ala
name:
--- 
- D-Ala-D-Ala dipeptidase
- D-alanyl-D-alanine dipeptidase
- vanX D-Ala-D-Ala dipeptidase
- VanX

comment:
A Zn2+-dependent enzyme [4]. The enzyme protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide (see diagram). This enzyme reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)-lactate (for which vancomycin has much less affinity) to be added to the cell wall instead [2,3]. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates [2]. Belongs in peptidase family M15.


entry: 3.4.14.1
name:
--- 
- dipeptidyl-peptidase I
- cathepsin C
- dipeptidyl aminopeptidase I
- dipeptidyl transferase
- dipeptide arylamidase I
- DAP I

comment:
A Cl--dependent, lysosomal cysteine-type peptidase maximally active at acidic pH. Also polymerizes dipeptide amides, arylamides and esters at neutral pH. In peptidase family C1 (papain family). Formerly EC 3.4.4.9

reaction:
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro


entry: 3.4.14.2
name:
--- 
- dipeptidyl-peptidase II
- dipeptidyl aminopeptidase II
- dipeptidyl arylamidase II
- carboxytripeptidase
- dipeptidyl peptidase II
- DAP II
- dipeptidyl(amino)peptidase II
- dipeptidylarylamidase

comment:
A lysosomal serine-type peptidase in family S28 (Pro-X carboxypeptidase family); maximally active at acidic pH

reaction:
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides


entry: 3.4.14.3
name: --- - Transferred to 3.4.19.1
comment:
Transferred entry: now EC 3.4.19.1 - Acylaminoacyl-peptidase (EC 3.4.14.3 created 1978, deleted 1981)


entry: 3.4.14.4
name:
--- 
- dipeptidyl-peptidase III
- dipeptidyl aminopeptidase III
- dipeptidyl arylamidase III
- enkephalinase B
- red cell angiotensinase

comment:
A cytosolic peptidase that is active at neutral pH. It has broad activity on peptides, although it is highly selective for Arg-Arg-2-naphthylamide, at pH 9.2. Active in the hydrolysis of enkephalins. A metallopeptidase, the type example of peptidase family M49.

reaction:
Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.


entry: 3.4.14.5
name:
--- 
- dipeptidyl-peptidase IV
- dipeptidyl aminopeptidase IV
- Xaa-Pro-dipeptidyl-aminopeptidase
- Gly-Pro naphthylamidase
- postproline dipeptidyl aminopeptidase IV
- lymphocyte antigen CD26
- glycoprotein GP110
- dipeptidyl peptidase IV
- glycylproline aminopeptidase
- X-prolyl dipeptidyl aminopeptidase
- pep X
- leukocyte antigen CD26
- glycylprolyl dipeptidylaminopeptidase
- dipeptidyl-peptide hydrolase
- glycylprolyl aminopeptidase
- dipeptidyl-aminopeptidase IV
- DPP IV/CD26
- amino acyl-prolyl dipeptidyl aminopeptidase
- T cell triggering molecule Tp103
- X-PDAP

comment:
A homodimer. An integral protein of the plasma membrane of lymphocytes and other mammalian cells, in peptidase family S9 (prolyl oligopeptidase family). The reaction is similar to that of the unrelated EC 3.4.14.11 Xaa-Pro dipeptidyl-peptidase of lactococci

reaction:
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline


entry: 3.4.14.6
name:
--- 
- dipeptidyl-dipeptidase
- dipeptidyl tetrapeptide hydrolase
- dipeptidyl ligase
- tetrapeptide dipeptidase

comment:
A thiol-activated peptidase from cabbage (Brassica oleracea). Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala

reaction:
Preferential release of dipeptides from a tetrapeptide, e.g. Ala-Gly-|-Ala-Gly. Acts more slowly on Ala-Ala-|-Ala-Ala and Gly-Gly-|-Gly-Gly


entry: 3.4.14.8
name: --- - Transferred to 3.4.14.9 and 3.4.14.10
comment:
Transferred entry: now EC 3.4.14.9 - tripeptidyl-peptidase I and EC 3.4.14.10 - tripeptidyl-peptidase II (EC 3.4.14.8 created 1989, deleted 1992)


entry: 3.4.14.9
name: --- - tripeptidyl-peptidase I - tripeptidyl aminopeptidase - tripeptidyl peptidase
reaction: Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
comment:
A lysosomal enzyme that is active at acidic pH. Deficient in classical late-infantile neuronal ceroid lipofuscinosis brain tissue. Belongs in peptidase family S53. Formerly included in EC 3.4.14.8.


entry: 3.4.14.10
reaction: Release of an N-terminal tripeptide from a polypeptide
name:
--- 
- tripeptidyl-peptidase II
- tripeptidyl aminopeptidase
- tripeptidyl peptidase
- tripeptidyl aminopeptidase II
- tripeptidyl peptidase II
- TPP

comment:
A cytosolic enzyme in peptidase family S8 (subtilisin family). Active at neutral pH. Inhibited by diisopropyl fluorophosphate. Formerly included in EC 3.4.14.8


entry: 3.4.14.11
name:
--- 
- Xaa-Pro dipeptidyl-peptidase
- X-prolyl dipeptidyl aminopeptidase
- PepX
- X-prolyl dipeptidyl peptidase
- X-Pro dipeptidyl-peptidase

comment:
The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15. The reaction is similar to that catalysed by dipeptidyl-peptidase IV of animals

reaction:
Hydrolyses Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile


entry: 3.4.14.12
name:
--- 
- Xaa-Xaa-Pro tripeptidyl-peptidase
- prolyltripeptidyl amino peptidase
- prolyl tripeptidyl peptidase
- prolyltripeptidyl aminopeptidase
- PTP-A
- TPP

comment:
This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease [1]. The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin 6. The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position [1]. The size of the peptide does not affect the rate of reaction [1].

reaction:
Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline


entry: 3.4.15.1
name:
--- 
- peptidyl-dipeptidase A
- angiotensin I-converting enzyme
- kininase II
- dipeptidyl carboxypeptidase I
- peptidase P
- carboxycathepsin
- dipeptide hydrolase
- peptidyl dipeptidase
- angiotensin converting enzyme
- dipeptidyl carboxypeptidase
- peptidyl dipeptidase I
- peptidyl-dipeptide hydrolase
- peptidyldipeptide hydrolase
- endothelial cell peptidyl dipeptidase
- ACE
- peptidyl dipeptidase-4
- peptidyl dipeptidase A
- PDH
- peptidyl dipeptide hydrolase
- DCP

comment:
A Cl--dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Type example of peptidase family M2

reaction:
Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II


entry: 3.4.15.2
name: --- - Transferred to 3.4.19.2
comment:
Transferred entry: now EC 3.4.19.2 - peptidyl-glycinamidase (EC 3.4.15.2 created 1978, deleted 1981)


entry: 3.4.15.3
name: --- - Transferred to 3.4.15.5
comment:
Transferred entry: now EC 3.4.15.5 - peptidyl-dipeptidase Dcp (EC 3.4.15.3 created 1981, modified 1989, deleted 1996)


entry: 3.4.15.4
reaction: Release of a C-terminal dipeptide or exceptionally a tripeptide
name:
--- 
- peptidyl-dipeptidase B
- dipeptidyl carboxyhydrolase
- atriopeptin convertase
- atrial di-(tri)peptidyl carboxyhydrolase
- peptidyldipeptidase B
- atrial dipeptidyl carboxyhydrolase
- atrial peptide convertase

comment:
A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence and shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II


entry: 3.4.15.5
name: --- - peptidyl-dipeptidase Dcp - dipeptidyl carboxypeptidase (Dcp) - dipeptidyl carboxypeptidase
comment:
Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3 (thimet oligopeptidase family). Ac-Ala-|-Ala-Ala is a good test substrate [3]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and included in EC 3.4.15.1, peptidyl-dipeptidase A."

reaction:
Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1' is Pro, or both P1 and P1' are Gly


entry: 3.4.16.1
name: --- - Transferred to 3.4.16.5 and 3.4.16.6
comment:
Transferred entry: now EC 3.4.16.5 - carboxypeptidase C, and EC 3.4.16.6 - carboxypeptidase D (EC 3.4.16.1 created 1972 as EC 3.4.12.1 and EC 3.4.21.13, both transferred 1978 to EC 3.4.16.1, deleted 1993)


entry: 3.4.16.2
reaction: Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid
name:
--- 
- lysosomal Pro-Xaa carboxypeptidase
- angiotensinase C
- lysosomal carboxypeptidase C
- peptidylprolylamino acid carboxypeptidase
- aminoacylproline carboxypeptidase
- prolyl carboxypeptidase
- carboxypeptidase P
- proline-specific carboxypeptidase P
- PCP

comment:
A lysosomal peptidase active at acidic pH that inactivates angiotensin II. Inhibited by diisopropyl fluorophosphate. In peptidase family S28 (Pro-X carboxypeptidase family). Formerly EC 3.4.12.4


entry: 3.4.16.3
name: --- - Transferred to 3.4.16.5
comment:
Transferred entry: now included with EC 3.4.16.5 - carboxypeptidase C [EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC 3.4.16.3, deleted 1992]


entry: 3.4.16.4
name:
--- 
- serine-type D-Ala-D-Ala carboxypeptidase
- DD-peptidase
- D-alanyl-D-alanine-carboxypeptidase
- D-alanyl-D-alanine-cleaving-peptidase
- D-alanyl-D-alanine-cleaving peptidase
- DD-transpeptidase
- D-alanine carboxypeptidase
- DD-carboxypeptidase
- D-alanyl carboxypeptidase

comment:
A membrane-bound, bacterial enzyme inhibited by penicillin and other beta-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase families S11, S12 and S13. Distinct from EC 3.4.17.14, zinc D-Ala-D-Ala carboxypeptidase

reaction:
Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine


entry: 3.4.16.5
reaction: Release of a C-terminal amino acid with broad specificity
name:
--- 
- carboxypeptidase C
- carboxypeptidase Y
- serine carboxypeptidase I
- cathepsin A
- lysosomal protective protein
- deamidase
- lysosomal carboxypeptidase A
- phaseolin

comment:
A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). Widely distributed in eukaryotes. Type example of peptidase family S10. Formerly EC 3.4.12.1 and EC 3.4.21.13, and included in EC 3.4.16.1.


entry: 3.4.16.6
reaction: Preferential release of a C-terminal arginine or lysine residue
name:
--- 
- carboxypeptidase D
- cereal serine carboxypeptidase II
- Saccharomyces cerevisiae KEX1 gene product
- carboxypeptidase Kex1
- gene KEX1 serine carboxypeptidase
- KEX1 carboxypeptidase
- KEX1 proteinase
- KEX1DELTAp
- CPDW-II

comment:
A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). In peptidase family S10 (carboxypeptidase C family). Formerly EC 3.4.12.1 and EC 3.4.21.13, and EC 3.4.16.1


entry: 3.4.17.1
reaction: Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
name:
--- 
- carboxypeptidase A
- carboxypolypeptidase
- pancreatic carboxypeptidase A
- tissue carboxypeptidase A

comment:
A zinc enzyme formed from procarboxypeptidase A. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells [3] and skeletal muscle [4]. Type example of peptidase family M14. Formerly EC 3.4.2.1 and EC 3.4.12.2


entry: 3.4.17.2
reaction: Preferential release of a C-terminal lysine or arginine amino acid
name:
--- 
- carboxypeptidase B
- protaminase
- pancreatic carboxypeptidase B
- tissue carboxypeptidase B
- peptidyl-L-lysine [L-arginine]hydrolase

comment:
A zinc enzyme formed from procarboxypeptidase B. Isolated from cattle, pig and dogfish pancreas and other sources, including skin fibroblasts [3] and adrenal medulla [4]. In peptidase family M14 (carboxypeptidase A family). Formerly EC 3.4.2.2 and EC 3.4.12.3


entry: 3.4.17.3
reaction: Release of a C-terminal basic amino acid, preferentially lysine
name:
--- 
- lysine carboxypeptidase
- carboxypeptidase N
- arginine carboxypeptidase
- kininase I
- anaphylatoxin inactivator
- plasma carboxypeptidase B
- creatine kinase conversion factor
- bradykinase
- kininase Ia
- hippuryllysine hydrolase
- bradykinin-decomposing enzyme
- protaminase
- CPase N
- creatinine kinase convertase
- peptidyl-L-lysine(-L-arginine) hydrolase
- CPN

comment:
A zinc enzyme found in plasma. Inactivates bradykinin and anaphylatoxins in blood plasma. In peptidase family M14 (carboxypeptidase A family). Formerly EC 3.4.12.7


entry: 3.4.17.4
name:
--- 
- Gly-Xaa carboxypeptidase
- glycine carboxypeptidase
- carboxypeptidase a
- carboxypeptidase S
- peptidase alpha
- yeast carboxypeptidase
- Gly-X carboxypeptidase

comment:
From yeast. In peptidase family M20 (glutamate carboxypeptidase family). Formerly EC 3.4.2.3, EC 3.4.12.8 and EC 3.4.17.9

reaction:
Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu


entry: 3.4.17.5
name: --- - Deleted entry
comment:
Deleted entry: aspartate carboxypeptidase [EC 3.4.17.5 created 1972 as EC 3.4.12.9, transferred 1978 to EC 3.4.17.5, deleted 1992]


entry: 3.4.17.6
name: --- - alanine carboxypeptidase - N-benzoyl-L-alanine-amidohydrolase
reaction: Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups
comment:
From soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid. Formerly EC 3.4.12.11


entry: 3.4.17.7
name: --- - Transferred to 3.5.1.28
comment:
Transferred entry: now EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase [EC 3.4.17.7 created 1978, deleted 1992]


entry: 3.4.17.8
iubmb_reaction: R04611
name:
--- 
- muramoylpentapeptide carboxypeptidase
- D-alanine carboxypeptidase I
- DD-carboxypeptidase
- D-alanine carboxypeptidase
- D-alanyl-D-alanine carboxypeptidase
- D-alanine-D-alanine-carboxypeptidase
- carboxypeptidase D-alanyl-D-alanine
- carboxypeptidase I
- UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase
- D-alanyl-D-alanine peptidase
- DD-peptidase
- penicillin binding protein 5
- PBP5
- PdcA
- VanY
- VanX (ambiguous)

comment:
A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D- alanine. Competitively inhibited by penicillins and cephalosporins.

reaction:
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D- alanyl-|-D-alanine [RN:R04611]


entry: 3.4.17.9
name: --- - Transferred to 3.4.17.4
comment:
Transferred entry: now included with EC 3.4.17.4 - Gly-Xaa carboxypeptidase [EC 3.4.17.9 created 1981, deleted 1992]


entry: 3.4.17.10
reaction: Release of C-terminal arginine or lysine residues from polypeptides
name:
--- 
- carboxypeptidase E
- carboxypeptidase H
- enkephalin convertase
- cobalt-stimulated chromaffin granule carboxypeptidase
- insulin granule-associated carboxypeptidase
- membrane-bound carboxypeptidase
- enkephalin-precursor endopeptidase
- enkephalin precursor carboxypeptidase
- peptidyl-L-lysine(-L-arginine) hydrolase

comment:
A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family). Formerly EC 3.4.17.10, carboxypeptidase H


entry: 3.4.17.11
name:
--- 
- glutamate carboxypeptidase
- carboxypeptidase G
- carboxypeptidase G1
- carboxypeptidase G2
- glutamyl carboxypeptidase
- N-pteroyl-L-glutamate hydrolase

comment:
A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20

reaction:
Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups


entry: 3.4.17.12
name: --- - carboxypeptidase M - CPM
reaction: Cleavage of C-terminal arginine or lysine residues from polypeptides
comment:
A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family)


entry: 3.4.17.13
name:
--- 
- muramoyltetrapeptide carboxypeptidase
- carboxypeptidase IIW
- carboxypeptidase II
- lysyl-D-alanine carboxypeptidase
- L-lysyl-D-alanine carboxypeptidase
- LD-carboxypeptidase

comment:
Variants are known from various microorganisms. Involved in peptidoglycan synthesis, catalysing both decarboxylation and transpeptidation. Stimulated by divalent cations such as Mg2+ and Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but unaffected by penicillin

reaction:
Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy- L-lysyl-|-D-alanine


entry: 3.4.17.14
reaction: Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-|-D-alanine
name:
--- 
- zinc D-Ala-D-Ala carboxypeptidase
- Zn2+ G peptidase, D-alanyl-D-alanine hydrolase
- D-alanyl-D-alanine-cleaving carboxypeptidase
- DD-carboxypeptidase
- G enzyme
- DD-carboxypeptidase-transpeptidase

comment:
A zinc enzyme. Catalyzes carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Weakly inhibited by beta-lactams. In peptidase family M15. Distinct from EC 3.4.16.4, serine-type D-Ala-D-Ala carboxypeptidase.


entry: 3.4.17.15
name: --- - carboxypeptidase A2 - CPA2
comment:
Isolated from rat pancreas but not present in cattle pancreas. In peptidase family M14 (carboxypeptidase A family)

reaction:
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues


entry: 3.4.17.16
comment: One of the renal brush border exopeptidases
reaction: Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
name:
--- 
- membrane Pro-Xaa carboxypeptidase
- carboxypeptidase P
- microsomal carboxypeptidase
- membrane Pro-X carboxypeptidase


entry: 3.4.17.17
comment: Active at neutral pH, from brain
name:
--- 
- tubulinyl-Tyr carboxypeptidase
- carboxypeptidase-tubulin
- soluble carboxypeptidase
- tubulin-tyrosine carboxypeptidase
- tubulin carboxypeptidase
- tubulinyltyrosine carboxypeptidase
- tyrosinotubulin carboxypeptidase
- tyrosyltubulin carboxypeptidase
- TTCPase
- brain I carboxypeptidase

reaction:
Cleavage of the -Glu-|-Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr


entry: 3.4.17.19
name: --- - carboxypeptidase Taq
reaction: Release of a C-terminal amino acid with broad specificity, except for -Pro
comment:
A 56-kDa enzyme from Thermus aquaticus. Most active at 80deg C. Type example of peptidase family M32


entry: 3.4.17.20
reaction: Release of C-terminal Arg and Lys from a polypeptide
name:
--- 
- carboxypeptidase U
- arginine carboxypeptidase
- carboxypeptidase R
- plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes)
- thrombin-activatable fibrinolysis inhibitor

comment:
Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family)


entry: 3.4.17.21
name:
--- 
- glutamate carboxypeptidase II
- N-acetylated-gamma-linked-acidic dipeptidase (NAALADase)
- folate hydrolase
- prostate-specific membrane antigen
- pteroylpoly-gamma-glutamate carboxypeptidase
- microsomal gamma-glutamyl carboxypeptidase
- pteroylpolyglutamate hydrolase
- folylpolyglutamate hydrolase
- pteroylpoly-gamma-glutamate hydrolase
- pteroylpolygammaglutamyl hydrolase
- pteroylpolyglutamic acid hydrolase
- PSM antigen
- acetylaspartylglutamate dipeptidase
- NAALA dipeptidase
- rat NAAG peptidase
- mGCP
- membrane glutamate carboxypeptidase
- N-acetylated-alpha-linked-amino dipeptidase
- prostrate-specific membrane antigen
- N-Acetylated alpha-linked acidic dipeptidase
- PSMA

comment:
A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa , but also exists in a soluble form. Hydrolyses alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu, and folylpoly-gamma-glutamates. With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate [4]. Does not hydrolyse Ac-beta-Asp-Glu. Known inhibitors: quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. Formerly EC 3.4.19.8. The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (gamma-Glu-X carboxypeptidase).

reaction:
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates


entry: 3.4.17.22
name: --- - metallocarboxypeptidase D - carboxypeptidase D (cattle, human, mouse, rat) - gp180 (duck)
reaction: Releases C-terminal Arg and Lys from polypeptides
comment:
Activated by Co2+; inhibited by guanidinoethylmercaptosuccinic acid. Large molecule (180 kDa) because of presence of three copies of metallopeptidase domain. The product of the silver gene (Drosophila) is similar. A zinc metallopeptidase in peptidase family M14 (carboxypeptidase A family)


entry: 3.4.18.1
name:
--- 
- cathepsin X
- cathepsin B2
- cysteine-type carboxypeptidase
- cathepsin IV
- cathepsin Z
- acid carboxypeptidase
- lysosomal carboxypeptidase B

comment:
Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13. Formerly EC 3.4.18.1, cysteine-type carboxypeptidase

reaction:
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity


entry: 3.4.19.1
reaction: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
name:
--- 
- acylaminoacyl-peptidase
- acylamino-acid-releasing enzyme
- N-acylpeptide hydrolase
- N-formylmethionine (fMet) aminopeptidase
- alpha-N-acylpeptide hydrolase

comment:
Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Formerly EC 3.4.14.3


entry: 3.4.19.2
reaction: Cleavage of C-terminal glycinamide from polypeptides
name:
--- 
- peptidyl-glycinamidase
- carboxyamidase
- peptidyl carboxy-amidase
- peptidyl-aminoacylamidase
- carboxamidopeptidase
- peptidyl amino acid amide hydrolase

comment:
Inactivates vasopressin and oxytocin by splitting off glycinamide. Also cleaves ester substrates of trypsin and chymotrypsin. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. The toad skin enzyme is inhibited by diisopropyl fluorophosphate. Formerly EC 3.4.15.2


entry: 3.4.19.3
name:
--- 
- pyroglutamyl-peptidase I
- 5-oxoprolyl-peptidase
- pyrase
- pyroglutamate aminopeptidase
- pyroglutamyl aminopeptidase
- L-pyroglutamyl peptide hydrolase
- pyrrolidone-carboxyl peptidase
- pyrrolidone-carboxylate peptidase
- pyrrolidonyl peptidase
- L-pyrrolidonecarboxylate peptidase
- pyroglutamidase
- pyrrolidonecarboxylyl peptidase

comment:
A cysteine peptidase, known from bacteria, plants and animals. The enzyme from bacterial sources is used in protein sequencing, and is the type example of peptidase family C15. Formerly EC 3.4.11.8

reaction:
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro


entry: 3.4.19.5
name: --- - beta-aspartyl-peptidase - beta-aspartyl dipeptidase - beta-aspartyl peptidase
reaction: Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
comment:
Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not hydrolysed. A mammalian, cytosolic enzyme. Formerly EC 3.4.13.10


entry: 3.4.19.6
name:
--- 
- pyroglutamyl-peptidase II
- thyroliberinase
- pyroglutamyl aminopeptidase II
- ", thyrotropin-releasing factor pyroglutamate aminopeptidase"
- pyroglutamate aminopeptidase II
- pyroglutamyl peptidase II
- thyroliberin-hydrolyzing pyroglutamate aminopeptidase
- thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase
- thyrotropin-releasing hormone-degrading peptidase
- TRH aminopeptidase

comment:
Highly specific for thyrotropin releasing hormone (pyroglutamyl-histidyl-prolylamide). Will not cleave the pyroglutamyl-histidyl bond of luteinizing hormone releasing hormone. Found in serum and brain. Inhibited by metal chelators. In peptidase family M1 (membrane alanyl aminopeptidase family)

reaction:
Release of the N-terminal pyroglutamyl group from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly tetrapeptides


entry: 3.4.19.7
name: --- - N-formylmethionyl-peptidase - (fMet)-releasing enzyme - formylmethionine aminopeptidase
reaction: Release of an N-terminal, formyl-methionyl residue from a polypeptide
comment:
Highly specific for N-formylmethionyl peptides. Will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine. Isolated from rat liver. Inhibited by heavy metals and activated by Cl-


entry: 3.4.19.8
name: --- - Transferred to 3.4.17.21
comment:
Transferred entry: now EC 3.4.17.21 - glutamate carboxypeptidase II (EC 3.4.19.8 created 1992, deleted 2000)


entry: 3.4.19.9
reaction: Hydrolysis of a gamma-glutamyl bond
iubmb_reaction: (other) R04242
kegg_reaction: R04242
name:
--- 
- gamma-glutamyl hydrolase
- conjugase
- folate conjugase
- lysosomal gamma-glutamyl carboxypeptidase
- gamma-Glu-X carboxypeptidase
- pteroyl-poly-gamma-glutamate hydrolase
- carboxypeptidase G
- folic acid conjugase
- poly(gamma-glutamic acid) endohydrolase
- polyglutamate hydrolase
- poly(glutamic acid) hydrolase II
- pteroylpoly-gamma-glutamyl hydrolase

comment:
A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Commonly studied with folylpoly-gamma-glutamate as substrate, with which the initial cleavage may release glutamate or poly-gamma-glutamate of two or more residues, according to the species of origin of the enzyme. Final products are pteroyl-alpha-glutamate (folic acid) and free glutamate. Highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group). Action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal gamma-Glu residue can be hydrolysed. Type example of peptidase family C26. Formerly EC 3.4.22.12


entry: 3.4.19.10
name: --- - Transferred to 3.5.1.28
comment:
Transferred entry: now EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase (EC 3.4.19.10 created 1972 as EC 3.4.12.5, transferred 1978 to EC 3.4.17.7, transferred 1992 to EC 3.4.19.10, deleted 1997)


entry: 3.4.19.11
name:
--- 
- gamma-D-glutamyl-meso-diaminopimelate peptidase
- endopeptidase I
- gamma-D-glutamyldiaminopimelate endopeptidase
- gamma-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase
- gamma-glutamyl-L-meso-diaminopimelyl endopeptidase
- gamma-D-glutamyl-meso-diaminopimelate endopeptidase
- gamma-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase
- gamma-D-glutamyl-meso-diaminopimelic endopeptidase
- gamma-D-glutamyl-meso-D-aminopimelic endopeptidase

comment:
A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family). Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism [3]

reaction:
Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted


entry: 3.4.19.12
name: --- - ubiquitinyl hydrolase 1 - ubiquitin C-terminal hydrolase - yeast ubiquitin hydrolase
comment:
Links to polypeptides smaller than 60 residues are hydrolysed more readily than those to larger polypeptides. Isoforms exist with quantitatively different specificities, amongst the best known being UCH-L1 and UCH-L3, which are major proteins of the brain of mammals [1]. Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). Ubiquitinyl hydrolase 1 is the type example of peptidase family C12, with a similar protein fold to papain and catalytic amino acids Cys, His and Asp. There is a separate family (C19) of enzymes that also hydrolyse ubiquitinyl bonds, and it is thought that all the ubiquitinyl hydrolases are also ubiquitin thiolesterases (EC 3.1.2.15)

reaction:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal)


entry: 3.4.21.1
reaction: Preferential cleavage: Tyr-|-, Trp-|-, Phe-|-, Leu-|-
name:
--- 
- chymotrypsin
- chymotrypsins A and B
- alpha-chymar ophth
- avazyme
- chymar
- chymotest
- enzeon
- quimar
- quimotrase
- alpha-chymar
- alpha-chymotrypsin A
- alpha-chymotrypsin

comment:
Chymotrypsin A is formed from cattle and pig chymotrypsinogen A, several iso-forms being produced according to the number of bonds hydrolysed in the precursor. Formerly EC 3.4.4.5. Chymotrypsin B, formerly EC 3.4.4.6, formed from chymotrypsinogen B, is homologous with chymotrypsin A. Enzymes with specificity similar to that of chymotrypsins A and B have been isolated from many species. In peptidase family S1 (trypsin family)


entry: 3.4.21.2
name: --- - chymotrypsin C
reaction: Preferential cleavage: Leu-|-, Tyr-|-, Phe-|-, Met-|-, Trp-|-, Gln-|-, Asn-|-
comment:
Formed from pig chymotrypsinogen C, and from cattle subunit II of procarboxypeptidase A. Reacts more readily with Tos-Leu-CH2Cl than Tos-Phe-CH2Cl in contrast to chymotrypsin. In peptidase family S1 (trypsin family)


entry: 3.4.21.4
reaction: Preferential cleavage: Arg-|-, Lys-|-
name:
--- 
- trypsin
- alpha-trypsin
- beta-trypsin
- cocoonase
- parenzyme
- parenzymol
- tryptar
- trypure
- pseudotrypsin
- tryptase
- tripcellim
- sperm receptor hydrolase

comment:
The single polypeptide chain cattle beta-trypsin is formed from trypsinogen by cleavage of one peptide bond. Further peptide bond cleavages produce alpha and other iso-forms. Isolated as multiple cationic and anionic trypsins [5] from the pancreas of many vertebrates and from lower species including crayfish, insects (cocoonase) and microorganisms (Streptomyces griseus) [3]. Type example of peptidase family S1. Formerly EC 3.4.4.4


entry: 3.4.21.5
name:
--- 
- thrombin
- fibrinogenase
- thrombase
- thrombofort
- topical
- thrombin-C
- tropostasin
- activated blood-coagulation factor II
- blood-coagulation factor IIa
- factor IIa
- E thrombin
- beta-thrombin
- gamma-thrombin

comment:
Formed from prothrombin. More selective than trypsin and plasmin. In peptidase family S1 (trypsin family). Formerly EC 3.4.4.13

reaction:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B


entry: 3.4.21.6
reaction: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin
name:
--- 
- coagulation factor Xa
- thrombokinase
- prothrombase
- prothrombinase
- activated blood-coagulation factor X
- autoprothrombin C
- thromboplastin
- plasma thromboplastin
- factor Xa
- activated Stuart-Prower factor
- activated factor X

comment:
Formed from the proenzyme factor X by limited proteolysis. In peptidase family S1 (trypsin family). Scutelarin (EC 3.4.21.60) has similar specificity


entry: 3.4.21.7
name: --- - plasmin - fibrinase - fibrinolysin - actase - serum tryptase - thrombolysin
comment:
Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin. In peptidase family S1 (trypsin family). Formerly EC 3.4.4.14

reaction:
Preferential cleavage: Lys-|- > Arg-|-; higher selectivity than trypsin. Converts fibrin into soluble products


entry: 3.4.21.8
name: --- - Transferred to 3.4.21.34 and 3.4.21.35
comment:
Transferred entry: now EC 3.4.21.34 - Plasma kallikrein and EC 3.4.21.35 - Tissue kallikrein (EC 3.4.21.8 created 1972, deleted 1981)


entry: 3.4.21.9
name: --- - enteropeptidase - enterokinase
reaction: Activation of trypsinogen by selective cleavage of Lys6-|-Ile bond
comment:
Is not inhibited by protein inhibitors of trypsin. In peptidase family S1 (trypsin family). Formerly EC 3.4.4.8


entry: 3.4.21.10
reaction: Preferential cleavage: Arg-|-, Lys-|-
name:
--- 
- acrosin
- acrosomal proteinase
- acrozonase
- alpha-acrosin
- beta-acrosin
- psi-acrosin
- acrosomal protease
- acrosin amidase

comment:
Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family)


entry: 3.4.21.11
name: --- - Transferred to 3.4.21.36 and 3.4.21.37
comment:
Transferred entry: now EC 3.4.21.36 - pancreatic elastase and EC 3.4.21.37 - leukocyte elastase (EC 3.4.21.11 created 1972, deleted 1981)


entry: 3.4.21.12
comment: From the myxobacterium Lysobacter enzymogenes. In peptidase family S1 (trypsin family)
reaction: Preferential cleavage: Ala-|-, Val-|- in bacterial cell walls, elastin and other proteins
name:
--- 
- alpha-lytic endopeptidase
- myxobacter alpha-lytic proteinase
- alpha-lytic proteinase
- alpha-lytic protease
- Mycobacterium sorangium alpha-lytic proteinase
- Myxobacter 495 alpha-lytic proteinase
- Myxobacter alpha-lytic proteinase


entry: 3.4.21.13
name: --- - Transferred to 3.4.16.5 and 3.4.16.6
comment:
Transferred entry: now EC 3.4.16.5, carboxypeptidase C and EC 3.4.16.6, carboxypeptidase D(EC 3.4.21.13 created 1972, deleted 1978)


entry: 3.4.21.14
name: --- - Transferred to 3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67
comment:
Transferred entry: now EC 3.4.21.62 - subtilisin; EC 3.4.21.63 - oryzin; EC 3.4.21.64 - endopeptidase K; EC 3.4.21.65 - thermomycolin; and EC 3.4.21.67 - endopeptidase So (EC 3.4.21.14 created 1961 as EC 3.4.4.16, transferred 1972 to EC 3.4.21.14, modified 1986, deleted 1992)


entry: 3.4.21.15
name: --- - Transferred to 3.4.21.63
comment:
Transferred entry: now EC 3.4.21.63 - oryzin (EC 3.4.21.15 created 1972, deleted 1978 [transferred to EC 3.4.21.14, deleted 1992])


entry: 3.4.21.17
name: --- - Deleted entry
comment:
Deleted entry: Arthrobacter serine proteinase (EC 3.4.21.17 created 1972, deleted 1978 [transferred to EC 3.4.21.14, deleted 1992])


entry: 3.4.21.18
name: --- - Deleted entry
comment:
Deleted entry: Tenebrio alpha-proteinase (EC 3.4.21.18 created 1972 [EC 3.4.99.24 created 1972, incorporated 1978], deleted 1992)


entry: 3.4.21.19
reaction: Preferential cleavage: Glu-|-, Asp-|-
name:
--- 
- glutamyl endopeptidase
- V8 proteinase
- endoproteinase Glu-C
- staphylococcal serine proteinase

comment:
From Staphylococcus aureus strain V8. In appropriate buffer the specificity is restricted to Glu-|-. In peptidase family S1 (trypsin family)


entry: 3.4.21.21
reaction: Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa
name:
--- 
- coagulation factor VIIa
- blood-coagulation factor VIIa
- activated blood coagulation factor VII

comment:
Formed from the precursor factor VII. The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human [1]. In peptidase family S1 (trypsin family)


entry: 3.4.21.22
reaction: Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa
name:
--- 
- coagulation factor IXa
- activated Christmas factor
- blood-coagulation factor IXa
- activated blood-coagulation factor IX
- autoprothrombin II
- blood platelet cofactor II
- activated blood coagulation factor XI

comment:
A chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa. In peptidase family S1 (trypsin family)


entry: 3.4.21.25
name: --- - cucumisin
reaction: Hydrolysis of proteins with broad specificity
comment:
From the sarcocarp of the musk melon (Cucumis melo). In peptidase family S8 (subtilisin family). Other endopeptidases from plants, which are less well characterized but presumably of serine-type, include euphorbain from Euphorbia cerifera ([6], formerly EC 3.4.21.56), solanain from horse-nettle Solanum elaeagnifolium ([1], formerly EC 3.4.99.21), hurain from Hura crepitans ([2], formerly EC 3.4.99.9) and tabernamontanain from Tabernamontana grandiflora ([3], formerly EC 3.4.99.23)


entry: 3.4.21.26
reaction: Hydrolysis of-Pro-|- and to a lesser extent-Ala-|- in oligopeptides
name:
--- 
- prolyl oligopeptidase
- post-proline cleaving enzyme
- proline-specific endopeptidase
- post-proline endopeptidase
- proline endopeptidase
- endoprolylpeptidase
- prolyl endopeptidase

comment:
Found in vertebrates, plants and Flavobacterium. Generally cytosolic, commonly activated by thiol compounds. Type example of peptidase family S9


entry: 3.4.21.27
reaction: Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa
name:
--- 
- coagulation factor XIa
- blood-coagulation factor XIa
- activated blood-coagulation factor XI
- activated plasma thromboplastin antecedent

comment:
In peptidase family S1 (trypsin family), and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor XI is activated by factor XIIa


entry: 3.4.21.28
name: --- - Transferred to 3.4.21.74
comment:
Transferred entry: now included with EC 3.4.21.74 - venombin A (EC 3.4.21.28 created 1978, deleted 1992)


entry: 3.4.21.29
name: --- - Transferred to 3.4.21.74
comment:
Transferred entry: now included with EC 3.4.21.74 - venombin A (EC 3.4.21.29 created 1978, deleted 1992)


entry: 3.4.21.30
name: --- - Transferred to 3.4.21.74
comment:
Transferred entry: now included with EC 3.4.21.74 - venombin A (EC 3.4.21.30 created 1978, deleted 1992)


entry: 3.4.21.31
name: --- - Transferred to 3.4.21.68 and 3.4.21.73
comment:
Transferred entry: now EC 3.4.21.68 - t-plasminogen activator and EC 3.4.21.73 - u-plasminogen activator (EC 3.4.21.31 created 1972 as EC 3.4.99.26, transferred 1978 to EC 3.4.21.31, deleted 1992)


entry: 3.4.21.32
name: --- - brachyurin - Uca pugilator collagenolytic proteinase - crab protease I - crab protease II
comment:
From hepatopancreas of the fiddler crab, Uca pugilator. In peptidase family S1 (trypsin family). Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidases from Uca pugilator [4], digestive enzymes from other decapod crustacea [5,6], and an enzyme from the fungus Entomophthora coronata (formerly EC 3.4.21.33) [1]

reaction:
Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin


entry: 3.4.21.34
name:
--- 
- plasma kallikrein
- serum kallikrein
- kininogenin
- kallikrein I
- kallikrein II
- kininogenase
- kallikrein
- callicrein
- glumorin
- padreatin
- padutin
- kallidinogenase
- bradykininogenase
- panceatic kallikrein
- onokrein P
- dilminal D
- depot-Padutin
- urokallikrein
- urinary kallikrein

comment:
Formed from plasma prokallikrein (Fletcher factor) by factor XIIa. Activates coagulation factors XII, VII and plasminogen. Selective for Arg > Lys in P1, in small molecule substrates. In peptidase family S1 (trypsin family). Formerly EC 3.4.4.21 and included in EC 3.4.21.8

reaction:
Selective cleavage of some Arg-|- and Lys-|- bonds, including Lys-|-Arg and Arg-|-Ser in (human) kininogen to release bradykinin


entry: 3.4.21.35
name:
--- 
- tissue kallikrein
- glandular kallikrein
- pancreatic kallikrein
- submandibular kallikrein
- submaxillary kallikrein
- kidney kallikrein
- urinary kallikrein
- kallikrein
- salivary kallikrein
- kininogenin
- kininogenase
- callicrein
- glumorin
- padreatin
- padutin
- kallidinogenase
- bradykininogenase
- depot-padutin
- urokallikrein
- dilminal D
- onokrein P

comment:
Formed from tissue prokallikrein by activation with trypsin. In peptidase family S1 (trypsin family). Formerly EC 3.4.4.21 and included in EC 3.4.21.8. A large number of tissue kallikrein-related sequences have been reported for rats [16] and mice [7], though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse gamma-renin (EC 3.4.21.54), submandibular proteinase A (formerly EC 3.4.21.40), [2,15], epidermal growth-factor-binding protein, nerve growth factor gamma-subunit, rat tonin [3,4,9], submaxillary proteinases A and B [10], T-kininogenase [18], kallikreins k7 and k8 [17] and human prostate-specific antigen (gamma-seminoprotein, [6])

reaction:
Preferential cleavage of Arg-|- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|- or Leu-|-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|- bonds [5]


entry: 3.4.21.36
reaction: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-
name:
--- 
- pancreatic elastase
- pancreatopeptidase E
- pancreatic elastase I
- elastase
- elaszym
- serine elastase

comment:
Formed by activation of proelastase from mammalian pancreas by trypsin. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.11


entry: 3.4.21.37
reaction: Hydrolysis of proteins, including elastin. Preferential cleavage Val-|- > Ala-|-
name:
--- 
- leukocyte elastase
- lysosomal elastase
- neutrophil elastase
- polymorphonuclear leukocyte elastase
- elastase
- elaszym
- serine elastase
- granulocyte elastase

comment:
Differs from pancreatic elastase in specificity on synthetic substrates and in inhibitor sensitivity. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.11


entry: 3.4.21.38
name:
--- 
- coagulation factor XIIa
- Hageman factor (activated)
- blood-coagulation factor XIIf
- activated beta blood-coagulation factor XII
- prealbumin activator
- Hageman factor beta-fragment
- Hageman factor fragment HFf
- blood-coagulation factor XIIabeta
- prekallikrein activator
- kallikreinogen activator

comment:
Also activates plasminogen and plasma prokallikrein. Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa. In peptidase family S1 (trypsin family)

reaction:
Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa


entry: 3.4.21.39
comment: In mast cell granules. In peptidase family S1 (trypsin family)
reaction: Preferential cleavage: Phe-|- > Tyr-|- > Trp-|- > Leu-|-
name:
--- 
- chymase
- mast cell protease I
- skeletal muscle protease
- skin chymotryptic proteinase
- mast cell serine proteinase, chymase
- skeletal muscle (SK) protease


entry: 3.4.21.41
name: --- - complement subcomponent C1r- - activated complement C1r - C1r- esterase
comment:
Activated from proenzyme C1r- in plasma during activation of the complement system by the "classical" route. In peptidase family S1 (trypsin family)

reaction:
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form C1s- (EC 3.4.21.42)


entry: 3.4.21.42
name: --- - complement subcomponent C1s- - C1 esterase - activated complement C1s - complement C1r-
comment:
Activated from proenzyme C1s in plasma by complement subcomponent C1r- . In peptidase family S1 (trypsin family)

reaction:
Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the "classical" pathway C3 convertase


entry: 3.4.21.43
name:
--- 
- classical-complement-pathway C3/C5 convertase
- C3 convertase
- C42-
- C4b,2a
- C5 convertase
- C423-
- C4b,2a,3b
- C42
- C423
- complement C.hivin.4.hivin2
- complement C3 convertase

comment:
A complex of complement fragments C4b, C2a and C2b. C2a contains the active site, C2b the site for C4b binding. C2a and C2b are formed by cleavage of proenzyme C2 by complement subcomponent C1s-. Cleavage of C5 requires complement fragment C3b which binds C5 and renders it susceptible to cleavage by the C4b,2a complex. Includes former EC 3.4.21.44. Complement component C2a is in peptidase family S1 (trypsin family)

reaction:
Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|- bond in complement component C5 alpha-chain to form C5a and C5b


entry: 3.4.21.44
name: --- - Transferred to 3.4.21.43
comment:
Transferred entry: now included with EC 3.4.21.43 - classical-complement-pathway C3/C5 convertase (EC 3.4.21.44 created 1981, deleted 1984)


entry: 3.4.21.45
reaction: Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage
name:
--- 
- complement factor I
- complement component C3b inactivator
- C3b inactivator
- C3b/C4b inactivator
- C3bINA
- complement C3b/C4b inactivator
- complement C4b inactivator
- conglutinogen-activating factor C
- complement C3b inactivator
- factor I
- complement C4bi

comment:
Cleavage of complement subcomponent C3b requires its binding to cofactor factor H or complement receptor CR1; cleavage of iC3b requires complement receptor CR1; cleavage of C4b requires C4b-binding protein. In peptidase family S1 (trypsin family)


entry: 3.4.21.46
name:
--- 
- complement factor D
- C3 proactivator convertase
- properdin factor D esterase
- factor D
- factor D (complement)

comment:
A component of the alternative pathway of complement activation. This reaction is analogous to the activation of complement component C2 by complement subcomponent C1s-. In peptidase family S1 (trypsin family)

reaction:
Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor


entry: 3.4.21.47
name:
--- 
- alternative-complement-pathway C3/C5 convertase
- complement component C3/C5 convertase (alternative)
- proenzyme factor B
- properdin factor B
- C3 proactivator
- glycine-rich beta-glycoprotein
- heat-labile factor
- C3 convertase
- C3b,Bb,CVF,Bb,C5 convertase
- (C3b)n,Bb
- complement C 3(C 5) convertase (amplification)
- alternative complement pathway C3(C5) convertase
- C5 convertase
- CVF,Bb
- (CVF)-dependent glycine-rich-beta-glucoprotein
- cobra venom factor-dependent C3 convertase

comment:
A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site. Bb is formed by cleavage of proenzyme factor B by factor D. Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex. C3b,Bb is stabilized in plasma by factor P. Complement factor B is in peptidase family S1 (trypsin family)

reaction:
Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|- bond in complement component C5 alpha-chain to yield C5a and C5b


entry: 3.4.21.48
name:
--- 
- cerevisin
- yeast proteinase B
- proteinase yscB
- baker's yeast proteinase B
- brewer's yeast proteinase
- peptidase beta

comment:
From Saccharomyces cerevisiae (baker's yeast, brewer's yeast). In peptidase family S8 (subtilisin family), but contains a Cys residue near the active site His, and is inhibited by mercurials. Proteinase ycaB is a similar enzyme from the yeast Candida albicans [3]

reaction:
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides


entry: 3.4.21.49
name: --- - hypodermin C - Hypoderma collagenase
comment:
From the larva of a warble fly, Hypoderma lineatum. Little action on small molecule substrates of trypsin, chymotrypsin, elastase or microbial collagenases. In peptidase family S1 (trypsin family)

reaction:
Hydrolysis of proteins including native collagen at -|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment


entry: 3.4.21.50
reaction: Preferential cleavage: Lys-|-, including -Lys-|-Pro-
name:
--- 
- lysyl endopeptidase
- Achromobacter proteinase I (also see Comment)
- Achromobacter lyticus alkaline proteinase I
- protease I
- achromopeptidase
- lysyl bond specific proteinase

comment:
From Achromobacter lyticus [6]. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C; [3]) and Pseudomonas aeruginosa (Ps-1; [4]). In peptidase family S1 (trypsin family)


entry: 3.4.21.52
name: --- - Deleted entry
comment:
Deleted entry: Cathepsin R (EC 3.4.21.52 created 1981 as EC 3.4.99.33, transferred 1984 to EC 3.4.21.52, deleted 1992)


entry: 3.4.21.53
reaction: Hydrolysis of proteins in presence of ATP
name:
--- 
- endopeptidase La
- ATP-dependent serine proteinase
- lon proteinase
- protease La
- proteinase La
- ATP-dependent lon proteinase
- ATP-dependent protease La
- Escherichia coli proteinase La
- Escherichia coli serine proteinase La
- gene lon protease
- gene lon proteins
- PIM1 protease
- PIM1 proteinase
- serine protease La

comment:
Product of the lon gene in Escherichia coli. ATP hydrolysis is linked with peptide bond hydrolysis; vanadate inhibits both reactions. Type example of peptidase family S16. A similar enzyme occurs in animal mitochondria


entry: 3.4.21.54
name: --- - gamma-renin
comment:
A member of the tissue kallikrein family, from submandibular glands of male mice. In peptidase family S1 (trypsin family)

reaction:
Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate (horse), to produce angiotensin I, but not active on natural angiotensinogen, unlike renin (EC 3.4.23.15). Also hydrolyses Bz-Arg-p-nitroanilide


entry: 3.4.21.55
name: --- - venombin AB - gabonase - okinaxobin II - Bitis gabonica venom serine proteinase - afaacytin
reaction: Selective cleavage at Arg-|- bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
comment:
From the venom of the Gaboon viper Bitis gabonica. Activates Factor XIII. Not inhibited by antithrombin III/heparin or hirudin, unlike EC 3.4.21.5, thrombin


entry: 3.4.21.56
name: --- - Deleted entry
comment:
Deleted entry: Euphorbain (EC 3.4.21.56 created 1972 as EC 3.4.99.7, transferred 1989 to EC 3.4.21.56, deleted 1992)


entry: 3.4.21.57
comment: From leaves of the spinach plant (Spinacia oleracea)
reaction: Hydrolysis of proteins. Preferential cleavage: Leu-|- in small molecule substrates
name:
--- 
- leucyl endopeptidase
- plant Leu-proteinase
- leucine-specific serine proteinase
- leucine endopeptidase
- spinach serine proteinase (leucine specific)
- spinach leucine-specific serine proteinase
- Leu-proteinase


entry: 3.4.21.59
reaction: Preferential cleavage: Arg-|-, Lys-|-, but with more restricted specificity than trypsin
name:
--- 
- tryptase
- mast cell tryptase
- mast cell protease II
- skin tryptase
- lung tryptase
- pituitary tryptase
- mast cell neutral proteinase
- mast cell serine proteinase II
- mast cell proteinase II
- mast cell serine proteinase tryptase
- rat mast cell protease II
- tryptase M

comment:
Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules. In peptidase family S1 (trypsin family). Not inhibited by alpha1-proteinase inhibitor or alpha2-macroglobulin


entry: 3.4.21.60
name: --- - scutelarin - taipan activator - Oxyuranus scutellatus prothrombin-activating proteinase
comment:
From the venom of the Taipan snake (Oxyuranus scutellatus). Converts prothrombin to thrombin in the absence of coagulation Factor Va, and is potentiated by phospholipid and Ca2+. Specificity is similar to that of Factor Xa. Binds Ca2+ via gamma-carboxyglutamic acid residues. Formerly EC 3.4.99.28. Similar enzymes are known from the venom of other Australian elapid snakes Pseudonaja textilis textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis

reaction:
Selective cleavage of Arg-|-Thr and Arg-|-Ile in prothrombin to form thrombin and two inactive fragments


entry: 3.4.21.61
name:
--- 
- kexin
- yeast KEX2 protease
- proteinase yscF
- prohormone-processing endoprotease
- paired-basic endopeptidase
- yeast cysteine proteinase F (misleading)
- andrenorphin-Gly-generating enzyme
- endoproteinase Kex2p
- gene KEX2 dibasic proteinase
- Kex 2p proteinase
- Kex2 endopeptidase
- Kex2 endoprotease
- Kex2 endoproteinase
- Kex2 protease
- proteinase Kex2p
- Kex2-like precursor protein processing endoprotease
- prohormone-processing KEX2 proteinase
- prohormone-processing proteinase
- proprotein convertase
- protease KEX2
- Kex2 proteinase
- Kex2-like endoproteinase

comment:
A Ca2+-activated peptidase of peptidase family S8, containing Cys near the active site His, and inhibited by p-mercuribenzoate. Similar enzymes occur in mammals. Formerly EC 3.4.22.23

reaction:
Cleavage of -Lys-Arg-|- and -Arg-Arg-|- bonds to process yeast alpha-factor pheromone and killer toxin precursors


entry: 3.4.21.62
name:
--- 
- subtilisin
- alcalase
- alcalase 0.6L
- alcalase 2.5L
- ALK-enzyme
- bacillopeptidase A
- bacillopeptidase B
- Bacillus subtilis alkaline proteinase bioprase
- bioprase AL 15
- bioprase APL 30
- colistinase
- (see also comments)
- subtilisin J
- subtilisin S41
- subtilisin Sendai
- subtilisin GX
- subtilisin E
- subtilisin BL
- genenase I
- esperase
- maxatase
- thermoase PC 10
- protease XXVII
- thermoase
- superase
- subtilisin DY
- subtilopeptidase
- SP 266
- savinase 8.0L
- savinase 4.0T
- kazusase
- protease VIII
- opticlean
- Bacillus subtilis alkaline proteinase
- protin A 3L
- savinase
- savinase 16.0L
- savinase 32.0 L EX
- orientase 10B
- protease S

comment:
Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Formerly EC 3.4.4.16 and included in EC 3.4.21.14. Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species [1,3]

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides


entry: 3.4.21.63
name:
--- 
- oryzin
- Aspergillus alkaline proteinase
- aspergillopeptidase B
- API 21
- aspergillopepsin B
- aspergillopepsin F
- Aspergillus candidus alkaline proteinase
- Aspergillus flavus alkaline proteinase
- Aspergillus melleus semi-alkaline proteinase
- Aspergillus oryzae alkaline proteinase
- Aspergillus parasiticus alkaline proteinase
- Aspergillus serine proteinase
- Aspergillus sydowi alkaline proteinase
- Aspergillus soya alkaline proteinase
- Aspergillus melleus alkaline proteinase
- Aspergillus sulphureus alkaline proteinase
- prozyme
- P 5380
- kyorinase
- seaprose S
- semi-alkaline protease
- sumizyme MP
- prozyme 10
- onoprose
- onoprose SA
- protease P
- promelase

comment:
A peptidase of family S8 (subtilisin family), not containing cysteine, that is the predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae. Formerly EC 3.4.21.15, and included in EC 3.4.21.14. Identical or closely related enzymes are produced by A. flavus and A. sojae [2,3,4]

reaction:
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides


entry: 3.4.21.64
name:
--- 
- peptidase K
- Tritirachium alkaline proteinase
- Tritirachium album serine proteinase
- proteinase K
- Tritirachium album proteinase K
- endopeptidase K

comment:
From the mold Tritirachium album Limber. A peptidase of family S8 (subtilisin family) containing two disulfide bridges and one free Cys near the active site His. Formerly included in EC 3.4.21.14

reaction:
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides


entry: 3.4.21.65
name: --- - thermomycolin - thermomycolase
comment:
A peptidase of family S8 (subtilisin family) from the thermophilic fungus Malbranchea pulchella var. sulfurea containing Cys, but not inhibited by p-mercuribenzoate. Very thermostable. Formerly included in EC 3.4.21.14

reaction:
Rather nonspecific hydrolysis of proteins. Preferential cleavage: Ala-|-, Tyr-|-, Phe-|- in small molecule substrates


entry: 3.4.21.66
reaction: Hydrolysis of proteins, including collagen
name:
--- 
- thermitase
- thermophilic Streptomyces serine proteinase
- Thermoactinomyces vulgaris serine proteinase

comment:
A peptidase of family S8 (subtilisin family) from Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate. The N-terminal extension of the polypeptide chain relative to subtilisin contributes to Ca2+-binding and the high thermostability. The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus (formerly included in EC 3.4.21.14) are closely similar [1,2]


entry: 3.4.21.67
reaction: Hydrolysis of proteins, but not Bz-Tyr-OEt, Ac-Phe-beta-naphthylester, or Bz-Arg-OEt
name:
--- 
- endopeptidase So
- E. coli cytoplasmic proteinase
- proteinase So
- Escherichia coli serine proteinase So

comment:
An Escherichia coli cytoplasmic endopeptidase formerly included in EC 3.4.21.14. Inhibited by Tos-Phe-CH2Cl, but not by Tos-Lys-CH2Cl


entry: 3.4.21.68
reaction: Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin
name:
--- 
- t-plasminogen activator
- tissue plasminogen activator
- plasminogen activator, tissue-type
- tissue-type plasminogen activator
- tPA
- t-PA

comment:
A peptidase of family S1 (trypsin family) from a wide variety of mammalian tissues, especially endothelial cells. Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin. Activity is considerably enhanced by fibrin. Formerly included in EC 3.4.21.31 and EC 3.4.99.26


entry: 3.4.21.69
reaction: Degradation of blood coagulation factors Va and VIIIa
name:
--- 
- protein C (activated)
- blood-coagulation factor XIVa
- activated blood coagulation factor XIV
- activated protein C
- autoprothrombin II-A
- protein Ca
- APC
- GSAPC

comment:
A peptidase of family S1 (trypsin family), one of the gamma-carboxyglutamic acid-containing coagulation factors. Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms


entry: 3.4.21.70
reaction: Preferential cleavage: Ala-|-. Does not hydrolyse elastin
name:
--- 
- pancreatic endopeptidase E
- cholesterol-binding proteinase
- proteinase E
- cholesterol-binding serine proteinase
- pancreatic protease E
- pancreatic proteinase E
- cholesterol-binding pancreatic proteinase
- CBPP
- pancreas E proteinase

comment:
A peptidase of family S1 (trypsin family) from pancreatic juice. Unlike elastases, has an acidic pI. Binds cholesterol


entry: 3.4.21.71
name: --- - pancreatic elastase II - pancreatic elastase 2
reaction: Preferential cleavage: Leu-|-, Met-|- and Phe-|-. Hydrolyses elastin
comment:
A peptidase of family S1 (trypsin family) formed by activation of proelastase II from mammalian pancreas by trypsin. Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II


entry: 3.4.21.72
name:
--- 
- IgA-specific serine endopeptidase
- IgA protease
- IgA proteinase
- IgA-specific proteinase
- immunoglobulin A protease
- immunoglobulin A proteinase

comment:
Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae. Type example of peptidase family S6. Some other bacterial endopeptidases with similar specificity are of metallo- type (see EC 3.4.24.13, IgA-specific metalloendopeptidase)

reaction:
Cleavage of immunoglobulin A molecules at certain Pro-|- bonds in the hinge region. No small molecule substrates are known


entry: 3.4.21.73
reaction: Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin
name:
--- 
- u-plasminogen activator
- urokinase
- urinary plasminogen activator
- cellular plasminogen activator
- urokinase-type plasminogen activator
- double-chain urokinase-type plasminogen activator
- two-chain urokinase-type plasminogen activator
- urokinase plasminogen activator
- uPA
- u-PA
- abbokinase
- urinary esterase A

comment:
Formed from the inactive precursor by action of plasmin or plasma kallikrein. Differs in structure from t-plasminogen activator (EC 3.4.21.68), and does not bind to fibrin. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.31 and EC 3.4.99.26


entry: 3.4.21.74
name:
--- 
- venombin A
- alpha-fibrinogenase
- habutobin
- zinc metalloproteinase Cbfib1.1
- zinc metalloproteinase Cbfib1.2
- zinc metalloproteinase Cbfib2
- ancrod
- (see also Comments)

comment:
A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper) (formerly EC 3.4.21.28) [1], batroxobin from Bothrops atrox (South American pit viper) (formerly EC 3.4.21.29) [2,5] and crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake) (formerly EC 3.4.21.30) [3,4]. In peptidase family S1 (trypsin family). Does not require activation by Ca2+

reaction:
Selective cleavage of Arg-|- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme


entry: 3.4.21.75
name:
--- 
- furin
- prohormone convertase
- dibasic processing enzyme
- PACE
- paired basic amino acid cleaving enzyme
- paired basic amino acid converting enzyme
- serine proteinase PACE
- PC1
- SPC3
- proprotein convertase

comment:
One of a group of peptidases in peptidase family S8 (subtilisin family) that is structurally and functionally similar to kexin. All are activated by Ca2+, contain Cys near the active site His, and are inhibited by p-mercuribenzoate. At least three related enzymes are recognized in mammals: PC2, PC3 and PC4, which have somewhat different specificities

reaction:
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|- bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors


entry: 3.4.21.76
reaction: Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|- > -Val-|-
name:
--- 
- myeloblastin
- leukocyte proteinase 3
- leukocyte proteinase 4
- Wegener's granulomatosis autoantigen
- proteinase PR-3
- proteinase-3
- PMNL proteinase

comment:
From polymorphonuclear leukocyte granules. In peptidase family S1 (trypsin family). Not inhibited by secretory leukocyte proteinase inhibitor


entry: 3.4.21.77
reaction: Preferential cleavage: -Tyr-|-
name:
--- 
- semenogelase
- prostate-specific antigen
- alpha-seminoprotein
- seminin
- P-30 antigen
- antigen (human clone lambdaHPSA-1 prostate-specific protein moiety reduced)
- gamma-seminoglycoprotein (human protein moiety reduced)
- gamma-SM
- antigen PSA (human prostate-specific)
- human glandular kallikrein
- antigen PSA (human clone 5P1 protein moiety reduced)

comment:
A peptidase of family S1 (trypsin family) from seminal plasma. Slowly inhibited by alpha1-antichymotrypsin


entry: 3.4.21.78
name:
--- 
- granzyme A
- CTLA3
- HuTPS
- T-cell associated protease 1
- cytotoxic T lymphocyte serine protease
- TSP-1
- T-cell derived serine proteinase

comment:
From cytotoxic T lymphocyte granules. In peptidase family S1 (trypsin family). The human enzyme does not cleave Phe-|--

reaction:
Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-, -Lys-|- >> -Phe-|- in small molecule substrates


entry: 3.4.21.79
comment: From cytotoxic T lymphocyte granules. In peptidase family S1 (trypsin family)
reaction: Preferential cleavage: -Asp-|- >> -Asn-|- > -Met-|-, -Ser-|-
name:
--- 
- granzyme B
- CTLA1
- CCPII
- cytotoxic cell proteinase-1
- granzyme G
- granzyme H
- CCP1 proteinase


entry: 3.4.21.80
reaction: Hydrolysis of proteins with specificity similar to chymotrypsin
name:
--- 
- streptogrisin A
- Streptomyces griseus protease A
- protease A
- proteinase A
- Streptomyces griseus proteinase A
- Streptomyces griseus serine proteinase 3
- Streptomyces griseus serine proteinase A

comment:
From Streptomyces griseus. A component of Pronase, in family S1 (trypsin family). Not inhibited by Tos-Phe-CH2Cl or ovomucoid


entry: 3.4.21.81
reaction: Hydrolysis of proteins with trypsin-like specificity
name:
--- 
- streptogrisin B
- Streptomyces griseus protease B
- pronase B
- serine proteinase B
- Streptomyces griseus proteinase B
- Streptomyces griseus proteinase 1
- Streptomyces griseus serine proteinase B

comment:
From Streptomyces griseus. A component of Pronase, in peptidase family S1 (trypsin family), distinct from Streptomyces trypsin


entry: 3.4.21.82
name: --- - glutamyl endopeptidase II - GluSGP
comment:
From Streptomyces griseus. A peptidase of family S1 (trypsin family). Inhibited by [Leu18->Glu]-modified turkey ovomucoid third domain

reaction:
Preferential cleavage: -Glu-|- >> -Asp-|- . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and -Glu-|-Pro- bonds is slow


entry: 3.4.21.83
name: --- - oligopeptidase B - protease II - Escherichia coli alkaline proteinase II
reaction: Hydrolysis of -Arg-|-, -Lys-|- bonds in oligopeptides, even when P1' residue is proline
comment:
Known from Escherichia coli. Inhibited by Tos-Lys-CH2Cl. In peptidase family S9 (prolyl oligopeptidase family)


entry: 3.4.21.84
name: --- - limulus clotting factor C- - factor C - limulus factor C
comment:
From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III. In peptidase family S1 (trypsin family)

reaction:
Selective cleavage of -Arg103-|-Ser- and -Ile124-|-Ile- bonds in limulus clotting factor B to form factor B-. Cleavage of -Pro-Arg-|- bonds in synthetic substrates


entry: 3.4.21.85
name: --- - limulus clotting factor B-
comment:
From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor B is activated by limulus clotting factor C-. In peptidase family S1 (trypsin family)

reaction:
Selective cleavage of -Arg98-|-Ile- bond in limulus proclotting enzyme to form active clotting enzyme


entry: 3.4.21.86
name: --- - limulus clotting enzyme - clotting enzyme
reaction: Selective cleavage of -Arg18-|- and -Arg47-|- bonds in coagulogen to form coagulin and fragments
comment:
From the hemocyte granules of horseshoe crabs Limulus and Tachypleus. Proclotting enzyme is activated by limulus clotting factor . In peptidase family S1 (trypsin family)


entry: 3.4.21.87
name: --- - Transferred to 3.4.23.49
comment:
Transferred entry: now EC 3.4.23.49, omptin. The enzyme is not a serine protease, as thought previously, but an aspartate protease. (EC 3.4.21.87 created 1993, deleted 2006)


entry: 3.4.21.88
name: --- - repressor LexA - LexA repressor
reaction: Hydrolysis of Ala84-|-Gly bond in repressor LexA
comment:
RecA protein and single-stranded DNA are required for activity, which is attributed to a Ser/Lys dyad [2]. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair. This peptidase activity of LexA was previously attributed to the RecA protein (formerly EC 3.4.99.37). Type example of peptidase family S24


entry: 3.4.21.89
name:
--- 
- signal peptidase I
- leader peptidase I
- signal proteinase
- Escherichia coli leader peptidase
- eukaryotic signal peptidase
- eukaryotic signal proteinase
- leader peptidase
- leader peptide hydrolase
- leader proteinase
- signal peptidase
- pilin leader peptidase
- SPC
- prokaryotic signal peptidase
- prokaryotic leader peptidase
- HOSP
- prokaryotic signal proteinase
- propeptidase
- PuIO prepilin peptidase
- signal peptide hydrolase
- signal peptide peptidase
- signalase
- bacterial leader peptidase 1

comment:
Present in the inner membrane of Escherichia coli. Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity [1,3]. Hydrolyses a single bond -Ala-|-Ala- in M13 phage procoat protein, producing free signal peptide and coat protein. Formerly included in EC 3.4.99.36. Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane [4] and mitochondrial inner membrane [2]. Type example of peptidase family S26

reaction:
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins


entry: 3.4.21.90
name: --- - togavirin - Sindbis virus protease - Sindbis virus core protein - NsP2 proteinase
comment:
Known from the Sindbis and Semliki forest togaviruses. Once released, the core protein does not retain catalytic activity. Togavirin is the type example of peptidase family S3 and has a similar tertiary structure to chymotrypsin [3]

reaction:
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond


entry: 3.4.21.91
name: --- - flavivirin - Yellow fever virus (flavivirus) protease - NS2B-3 proteinase
comment:
Known from classical flaviviruses (yellow fever, dengue fever). The functional viral peptidase is part of the NS2B protein. Catalytic His, Asp and Ser residues are arranged as in chymotrypsin, but flavivrin is the type example of peptidase family S7

reaction:
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala


entry: 3.4.21.92
name:
--- 
- endopeptidase Clp
- endopeptidase Ti
- caseinolytic protease
- protease Ti
- ATP-dependent Clp protease
- ClpP
- Clp protease

comment:
An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2 [4]. ClpP is the type example of peptidase family S14

reaction:
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs)


entry: 3.4.21.93
name: --- - proprotein convertase 1 - prohormone convertase 3 - neuroendocrine convertase 1 - PC1
comment:
A Ca2+-dependent enzyme, maximally active at about pH 5.5. Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. Unlike prohormone convertase 2, does not hydrolyse proluteinizing-hormone-releasing-hormone. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 2. In peptidase family S8 (subtilisin family)

reaction:
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds


entry: 3.4.21.94
name: --- - proprotein convertase 2 - neuroendocrine convertase 2 - PC2
comment:
A Ca2+-dependent enzyme, maximally active at about pH 5.5. Specificity is broader than that of prohormone convertase 1. Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proglucagon, proinsulin and proluteinizing-hormone-releasing-hormone. Does not hydrolyse prorenin or prosomatostatin, however. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 1. In peptidase family S8 (subtilisin family)

reaction:
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds


entry: 3.4.21.95
name: --- - snake venom factor V activator
comment:
Known from venom of Vipera russelli. Inhibited by di-isopropyl fluorophosphate, unlike the metallopeptidase russellysin (EC 3.4.24.58) that is specific for factor X [1]. In peptidase family S1 (trypsin family) [2]

reaction:
Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545-|-Ser-Asn-Asn-Gly bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg- OEt and Tos-Arg- OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2


entry: 3.4.21.96
name:
--- 
- lactocepin
- CEP
- extracellular lactococcal proteinase
- lactococcal cell wall-associated proteinase
- lactococcal cell envelope-associated proteinase
- lactococcal proteinase
- PrtP

comment:
associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence. Responsible for the hydrolysis of casein in milk and the provision of peptides essential to cell growth. Important in cheese making and the production of lactic casein, being required for rapid growth to high cell densities with concomitant production of adequate levels of lactic acid. Specificity differences between lactocepins from different starter strains may be partly responsible for imparting different flavour qualities to cheese [4]. In peptidase family S8 (subtilisin family)

reaction:
Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position [1,2] Best known for its action on caseins, although it has been shown to hydrolyse haemoglobin and oxidised insulin B chain


entry: 3.4.21.97
name: --- - assemblin
reaction: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein
comment:
Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Inhibited by diisopropyl fluorophosphate. Type example of peptidase family S21. Catalytic residues are His, Ser, His, a combination not known for any other peptidase, and the protein fold also is unique. Known from herpes viruses of several types, cytomegalovirus, Epstein-Barr virus and human herpesvirus 3


entry: 3.4.21.98
name:
--- 
- hepacivirin
- Cpro-2
- hepatitis C virus NS3 serine proteinase
- NS3-4A serine proteinase complex

comment:
Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. Type example of peptidase family S29. The crystallographic structure shows a chymotrypsin-like fold

reaction:
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'


entry: 3.4.21.99
name: --- - spermosin
reaction: Hydrolyses arginyl bonds, preferably with Pro in the P2 position
comment:
The enzyme from the ascidian (Prochordate) Halocynthia roretzi is localised in the sperm head, and released during sperm activation. A proline-rich region is involved in binding to the vitelline coat of the egg. Belongs in peptidase family S1 (trypsin family).


entry: 3.4.21.100
name:
--- 
- pseudomonalisin
- Pseudomonas sp. pepstatin-insensitive carboxyl proteinase
- pseudomonapepsin

comment:
An enzyme secreted by Pseudomonas sp. No. 101. Optimum pH is 4. It is distinguished from xanthomonapepsin by its insensitivity to EPNP and from scytalidopepsin B by this property and by its unrelated amino-acid sequence. Inhibited by tyrostatin, a peptide aldehyde [2]. Type example of peptidase family S53.

reaction:
Hydrolysis of the B chain of insulin at -Glu13-|-Ala-, -Leu15-|-Tyr- and -Phe25-|-Tyr-, and angiotensin I at -Tyr4-|-Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO2)-Arg-Leu.


entry: 3.4.21.102
name:
--- 
- C-terminal processing peptidase
- CtpA gene product (Synechocystis sp.)
- photosystem II D1 protein processing peptidase
- protease Re
- tail-specific protease
- Tsp protease

comment:
Proteolytic processing of the D1 protein of photosystem II is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The recognition of the substrate is mediated by a PDZ domain, a small protein module that promotes protein-protein interactions by binding to internal or C-terminal sequences of their partner proteins. Type example of peptidase family S41.

reaction:
The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II


entry: 3.4.21.103
name:
--- 
- physarolisin
- Dictyostelium discoideum aspartic proteinase
- Dictyostelium discoideum aspartic proteinase E
- Physarum flavicomum aspartic proteinase
- Physarum polycephalum acid proteinase
- Physarum aspartic proteinase
- physaropepsin

comment:
Belongs in peptidase family S53. From the slime mold Physarum polycephalum. Is not inhibited by pepstatin, but is blocked by methyl 2-diazoacetamidohexanoate. Closely similar enzymes are found in Dictyostelium discoideum and P. flavicomum. Formerly included in EC 3.4.23.6.

reaction:
Milk clotting activity. Preferential cleavage of Gly8-|-Ser in B chain of insulin most rapidly, followed by Leu11-|-Val, Cys(SO3H)19-|-Gly and Phe24-|-Phe. No action on Ac-Phe-Tyr(I)2.


entry: 3.4.21.104
name:
--- 
- mannan-binding lectin-associated serine protease-2
- MASP-2
- MBP-associated serine protease-2
- mannose-binding lectin-associated serine protease-2
- p100
- mannan-binding lectin-associated serine peptidase

comment:
Mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine, on a wide range of microbial surfaces and is able to initiate activation of the lectin pathway of complement [7]. This enzyme displays C1s--like esterolytic activity (cf. EC 3.4.21.42, complement subcomponent C1s-). It also cleaves C4 and C2 with efficiencies that are relatively higher than those of EC 3.4.21.42 [3]. Belongs in peptidase family S1A.

reaction:
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile)


entry: 3.4.21.105
name: --- - rhomboid protease
comment:
These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. A catalytic dyad is involved in proteolysis rather than a catalytic triad, as was thought previously [14]. They are important for embryo development in Drosophila melanogaster. Rhomboid is a key regulator of EGF receptor signalling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Belongs in peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Rhomboids are widely conserved from bacteria to archaea to humans [9,13].

reaction:
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains


entry: 3.4.21.106
name: --- - hepsin
reaction: Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys
comment:
This type-II membrane-associated serine peptidase has been implicated in cell growth and development [1,3]. The enzyme has been shown to activate blood coagulation factor VII by cleavage of the Arg152-|-Ile153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation [2]. There is no cleavage after aromatic or aliphatic residues [1]. The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue. The nature of the residue at S3 also affects hydrolysis, with Gln being much more favourable than Ala [1]. Belongs in peptidase family S1A.


entry: 3.4.21.107
name:
--- 
- peptidase Do
- DegP
- DegP protease
- HtrA
- high temperature requirement protease A
- HrtA heat shock protein
- protease Do
- Do protease

comment:
This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E. coli [3]. The enzyme has weak peptidase activity with casein and other non-native substrates [3]. The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures [1,6]. Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme [6]. Belongs in peptidase family S1C.

reaction:
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val


entry: 3.4.21.108
name:
--- 
- HtrA2 peptidase
- high temperature requirement protein A2
- HtrA2
- Omi stress-regulated endoprotease
- serine proteinase OMI
- HtrA2 protease
- OMI/HtrA2 protease
- HtrA2/Omi
- Omi/HtrA2

comment:
This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment [4]. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP) [3]. Belongs in peptidase family S1C.

reaction:
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues


entry: 3.4.21.109
name:
--- 
- matriptase
- serine protease 14
- membrane-type serine protease 1
- MT-SP1
- prostamin
- serine protease TADG-15
- tumor-associated differentially-expressed gene 15 protein
- ST14
- breast cancer 80 kDa protease
- epithin
- serine endopeptidase SNC19

comment:
This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis [1,2]. The enzyme can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active alpha- and beta-HGF, but It does not activate plasminogen, which shares high homology with HGF [1]. The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade [1,2]. Belongs in peptidase family S1A.

reaction:
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position


entry: 3.4.21.110
name: --- - C5a peptidase - streptococcal C5a peptidase - ScpA - ScpB - SCPA
comment:
This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate specificity. Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties [1,4]. Belongs in peptidase family S8A.

reaction:
The primary cleavage site is at His67-|-Lys68 in human C5a with a minor secondary cleavage site at Ala58-|-Ser59


entry: 3.4.21.111
name: --- - aqualysin 1 - caldolysin
comment:
This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase. It has three subsites, S1, S2, and S3, in the substrate binding site. The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile [3]. These specificities are similar to those of EC 3.4.21.64 (peptidase K) and EC 3.4.21.62 (subtilisin BPN') [3]. The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyses elastin substrates such as succinyl-(Ala)n-p-nitroanilide (n = 1,2,3) and some peptide esters [1,3]. Belongs in peptidase family S8A.

reaction:
Exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position


entry: 3.4.21.112
name:
--- 
- site-1 protease
- mammalian subtilisin/kexin isozyme 1
- membrane-bound transcription factor site-1 protease
- proprotein convertase SKI-1
- proprotein convertase SKI-1/S1PPS1
- S1P endopeptidase
- S1P protease
- site-1 peptidase
- SKI-1
- SREBP proteinase
- SREBP S1 protease
- SREBP-1 proteinase
- SREBP-2 proteinase
- sterol regulatory element-binding protein proteinase
- sterol regulatory element-binding protein site 1 protease
- sterol-regulated luminal protease
- subtilase SKI-1
- subtilase SKI-1/S1P
- subtilisin/kexin-isozyme 1

comment:
Cleaves sterol regulatory element-binding proteins (SREBPs) and thereby initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholesterol and unsaturated fatty acids into the bloodstream [1]. The enzyme also processes pro-brain-derived neurotrophic factor and undergoes autocatalytic activation in the endoplasmic reticulum through sequential cleavages [5]. The enzyme can also process the unfolded protein response stress factor ATF6 at an Arg-His-Lys-Lys-|- site [4,8], and the envelope glycoprotein of the highly infectious Lassa virus [5,8] and Crimean Congo haemorrhagic fever virus at Arg-Arg-Lys-Lys-|- [7,8]. Belongs in peptidase family S8A.

reaction:
Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3


entry: 3.4.21.113
name:
--- 
- pestivirus NS3 polyprotein peptidase
- border disease virus NS3 endopeptidase
- BDV NS3 endopeptidase
- bovine viral diarrhea virus NS3 endopeptidase
- BVDV NS3 endopeptidase
- classical swine fever virus NS3 endopeptidase
- CSFV NS3 endopeptidase
- p80

comment:
The polyprotein of noncytopathogenic pestiviruses is cleaved co- and post-translationally into at least 11 proteins (N(pro), C, E(rns), E1, E2, p7, NS2-3, NS4A, NS4B, NS5A, and NS5B) [2]. The genomes of cytopathogenic pestivirus strains express at least one additional protein, called NS3 (p80) [2]. This enzyme, which resides in the N-terminal region of NS3 (nonstructural protein 3), is essential for generation of its own C-terminus and for processing of the downstream cleavage sites, leading to the release of the pestivirus nonstructural proteins NS4A, NS4B, NS5A and NS5B [1,2]. Belongs in peptidase family S31.

reaction:
Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites


entry: 3.4.21.114
name: --- - equine arterivirus serine peptidase
comment:
In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12) [3]. It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position [1]. Cleavage of ORF1ab by this enzyme is essential for viral replication [2]. Belongs in peptidase family S32.

reaction:
Cleavage of (Glu/Gln)-|-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab


entry: 3.4.21.115
name:
--- 
- infectious pancreatic necrosis birnavirus Vp4 peptidase
- infectious pancreatic necrosis virus protease
- IPNV Vp4 protease
- IPNV Vp4 peptidase
- NS protease
- NS-associated protease
- Vp4 protease

comment:
Infectious pancreatic necrosis virus (IPNV) is a birnavirus that causes an acute, contagious disease in young salmonid fish [2]. As with most viruses that infect eukaryotic cells, the proteolytic processing of viral precursor proteins is a crucial step in the life cycle of this virus [2]. pVP2 is converted into VP2 by cleavage near the carboxy end of pVP2. This cleavage is most likely due to host-cell proteases rather than VP4 [2,3]. Differs from most serine peptidases in not having the catalytic triad Ser-His-Asp [2]. Belongs in peptidase family S50.

reaction:
Cleaves the (Ser/Thr)-Xaa-Ala-|-(Ser/Ala)-Gly motif in the polyprotein NH2-pVP2-VP4-VP3-COOH of infectious pancreatic necrosis virus at the pVP2-VP4 and VP4-VP3 junctions


entry: 3.4.21.116
name: --- - SpoIVB peptidase - sporulation factor IV B protease
reaction: Self-cleaves Val52-|-Asn53, Ala62-|-Phe63 and Val74-|-Thr75 at the N-terminus of SpoIVB
comment:
This enzyme plays a central role in a regulatory checkpoint (the &sigma;K checkpoint), which coordinates gene expression during the later stages of spore formation in Bacillus subtilis [1,3]. The enzyme activates proteolytic processing of a sporulation-specific sigma factor, pro-&sigma;K, to its mature and active form, &sigma;K, by self-cleavage [1,3]. The enzyme is also subject to secondary proteolysis, which presumably inactivates SpoIVB [3]. The enzyme is also essential for the formation of heat-resistant spores. Belongs in peptidase family S55.


entry: 3.4.21.117
name: --- - stratum corneum chymotryptic enzyme - kallikrein 7 - SCCE - KLK7 - PRSS6 - hK7
reaction: Cleavage of proteins with aromatic side chains in the P1 position
comment:
This enzyme has wide substrate specificity, being able to degrade heat-denatured bovine casein and the alpha-chain of native human fibrinogen. It cleaves the B chain of bovine insulin at Leu6-|-Cya7, Tyr16-|-Leu17, Phe25-|-Tyr26 and Tyr26-|-Thr27 [1]. It is thought to play a role in the desquamation (skin-shedding) of the outer layer of skin, the stratum corneum, by degrading intercellular cohesive structures [1,2]. Belongs in peptidase family S1A.


entry: 3.4.21.118
name:
--- 
- kallikrein 8
- KLK8
- PRSS19
- human kallikrein 8
- hK8
- mK8
- ovasin
- tumor-associated differentially expressed gene 14
- TADG-14
- NP
- neuropsin

comment:
The enzyme is activated by removal of an N-terminal prepropeptide [2,4]. The highest amidolytic activity is observed using Boc-Val-Pro-Arg-|-7-amido-4-methylcoumarin, which is a substrate of alpha-thrombin [2,4]. Substrates lacking basic amino acids in the P1 position are not cleaved [4]. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen [3] and is associated with diseases such as ovarian cancer and Alzheimer's disease [4]. Belongs in peptidase family S1A.

reaction:
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys


entry: 3.4.21.119
name:
--- 
- kallikrein 13
- KLK13
- kallikrein mK13
- mGK-13
- mK13
- mKLK13
- prorenin converting enzyme 1
- PRECE-1
- prorenin-converting enzyme
- PRECE
- proteinase P

comment:
The enzyme is specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates [1]. Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used. This enzyme is also able to process pro-interleukin-1beta (pro-IL-1beta) in mouse submandibular gland to form IL-1beta [4]. Belongs in peptidase family S1A.

reaction:
Hydrolyses mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin


entry: 3.4.22.1
name: --- - cathepsin B - cathepsin B1 (obsolete) - cathepsin II
comment: An intracellular (lysosomal) enzyme in peptidase family C1 (papain family)
reaction:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides


entry: 3.4.22.2
name: --- - papain - papayotin - summetrin - velardon - papaine - Papaya peptidase I
comment:
Type example of peptidase family C1 from latex of the papaya (Carica papaya) fruit. Inhibited by compound E-64 and proteins of the cystatin family. Formerly EC 3.4.4.10

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'


entry: 3.4.22.3
name: --- - ficain - ficin - debricin - higueroxyl delabarre
reaction: Similar to that of papain
comment:
The major proteolytic component of the latex of fig, Ficus glabrata. Cysteine endopeptidases with similar properties are present in other members of the large genus Ficus. In peptidase family C1 (papain family). Formerly EC 3.4.4.12


entry: 3.4.22.4
name: --- - Transferred to 3.4.22.32 and 3.4.22.33
comment:
Transferred entry: now EC 3.4.22.32 - stem bromelain, and EC 3.4.22.33 - fruit bromelain (EC 3.4.22.4 created 1972, deleted 1992 [EC 3.4.22.5 created 1972, incorporated 1978])


entry: 3.4.22.6
name: --- - chymopapain - chymopapain A - chymopapain B - chymopapain S
reaction: Similar to that of papain
comment:
The major endopeptidase of papaya (Carica papaya) latex. It has multiple chromatographic forms. In peptidase family C1 (papain family). Formerly EC 3.4.4.11


entry: 3.4.22.7
name: --- - asclepain
reaction: Similar to that of papain
comment:
From the latex of milkweed, Asclepias syriaca. It has multiple forms, and is in peptidase family C1 (papain family)


entry: 3.4.22.8
reaction: Preferential cleavage: Arg-|-, including Arg-|-Pro, but not Lys-
name:
--- 
- clostripain
- clostridiopeptidase B
- clostridium histolyticum proteinase B
- alpha-clostridipain
- clostridiopeptidase

comment:
From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11. Formerly EC 3.4.4.20


entry: 3.4.22.10
reaction: Preferential cleavage with hydrophobic residues at P2, P1 and P1'
name:
--- 
- streptopain
- Streptococcus peptidase A
- streptococcal cysteine proteinase
- Streptococcus protease

comment:
From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Type example of peptidase family C10. Formerly EC 3.4.4.18


entry: 3.4.22.11
name: --- - Transferred to 3.4.24.56
comment:
Transferred entry: now EC 3.4.24.56 - insulysin (EC 3.4.22.11 created 1976, deleted 1978 [transferred to EC 3.4.99.45, deleted 1993])


entry: 3.4.22.12
name: --- - Transferred to 3.4.19.9
comment:
Transferred entry: now EC 3.4.19.9 - gamma-Glu-X carboxypeptidase (EC 3.4.22.12 created 1978, deleted 1992)


entry: 3.4.22.13
name: --- - Deleted entry
comment:
Deleted entry: staphylococcal cysteine proteinase (EC 3.4.22.13 created 1978, modified 1981, deleted 1992)


entry: 3.4.22.14
name: --- - actinidain - actinidin - Actinidia anionic protease - proteinase A2 of Actinidia chinensis
reaction: Similar to that of papain
comment:
From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In peptidase family C1 (papain family)


entry: 3.4.22.15
name: --- - cathepsin L - Aldrichina grahami cysteine proteinase
comment:
A lysosomal enzyme in peptidase family C1 (papain family) that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64

reaction:
Similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity


entry: 3.4.22.16
comment: Present in lysosomes of mammalian cells. In peptidase family C1 (papain family)
name:
--- 
- cathepsin H
- cathepsin B3
- benzoylarginine-naphthylamide (BANA) hydrolase (obsolete)
- cathepsin Ba, aleurain
- N-benzoylarginine-beta-naphthylamide hydrolase

reaction:
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|- bonds) as well as an endopeptidase


entry: 3.4.22.17
name: --- - Transferred to 3.4.22.52 and 3.4.22.53
comment:
Transferred entry: now EC 3.4.22.52, calpain-1 and EC 3.4.22.53, calpain-2 (EC 3.4.22.17 created 1981 [EC 3.4.24.5 created 1978, part incorporated 1989], deleted 2003)


entry: 3.4.22.18
name: --- - Transferred to 3.4.21.26
comment:
Transferred entry: now included with EC 3.4.21.26 - prolyl oligopeptidase (EC 3.4.22.18 created 1981, deleted 1992)


entry: 3.4.22.19
name: --- - Transferred to 3.4.24.15
comment:
Transferred entry: now included with EC 3.4.24.15 - thimet oligopeptidase (EC 3.4.22.19 created 1989, deleted 1992)


entry: 3.4.22.21
name: --- - Transferred to 3.4.99.46
comment:
Transferred entry: now included with EC 3.4.99.46 - multicatalytic endopeptidase complex (EC 3.4.22.21 created 1989, deleted 1992)


entry: 3.4.22.24
name: --- - cathepsin T
reaction: Interconversion of the three forms of tyrosine aminotransferase, EC 2.6.1.5
comment:
Degrades azocasein and denatured hemoglobin; the only native protein on which it has been shown to act is tyrosine aminotransferase


entry: 3.4.22.25
reaction: Preferential cleavage: Gly-|-, in proteins and small molecule substrates
name:
--- 
- glycyl endopeptidase
- papaya peptidase B
- papaya proteinase IV
- glycine-specific proteinase
- chymopapain
- Papaya proteinase 4
- PPIV
- chymopapain M

comment:
From the papaya plant, Carica papaya. Not inhibited by chicken cystatin, unlike most other homologues of papain, but in peptidase family C1 (papain family)


entry: 3.4.22.27
name: --- - cathepsin S
comment:
A lysosomal cysteine endopeptidase that is unusual amongst such enzymes for its stability to neutral pH. In peptidase family C1 (papain family)

reaction:
Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|- compound


entry: 3.4.22.28
name:
--- 
- picornain 3C
- picornavirus endopeptidase 3C
- poliovirus protease 3C
- rhinovirus protease 3C
- foot-and-mouth protease 3C
- poliovirus proteinase 3C
- rhinovirus proteinase 3C
- coxsackievirus 3C proteinase
- foot-and-mouth-disease virus proteinase 3C
- 3C protease
- 3C proteinase
- cysteine proteinase 3C
- hepatitis A virus 3C proteinase
- protease 3C
- tomato ringspot nepovirus 3C-related protease

comment:
From entero-, rhino-, aphto- and cardioviruses. Larger than the homologous virus picornain 2A. Type example of peptidase family C3

reaction:
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly


entry: 3.4.22.29
reaction: Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein
name:
--- 
- picornain 2A
- picornavirus endopeptidase 2A
- poliovirus protease 2A
- rhinovirus protease 2A
- 2A protease
- 2A proteinase
- protease 2A
- proteinase 2Apro
- picornaviral 2A proteinase
- Y-G proteinase 2A
- poliovirus proteinase 2A
- poliovirus protease 2Apro

comment:
From entero-, rhino-, aphto- and cardioviruses. Smaller than the homologous picornain 3C, which is also in peptidase family C3 (picornain 3C family)


entry: 3.4.22.30
comment: From papaya plant, Carica papaya. In peptidase family C1 (papain family)
name:
--- 
- caricain
- papaya peptidase A
- papaya peptidase II
- papaya proteinase Omega
- papaya proteinase III
- papaya proteinase 3
- proteinase Omega
- papaya proteinase A
- chymopapain S
- PpOmega

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain


entry: 3.4.22.31
name: --- - ananain - stem bromelain - fruit bromelain
comment:
From stem of pineapple plant, Ananas comosus. Differs from stem and fruit bromelains in being inhibited by chicken cystatin. In peptidase family C1 (papain family)

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain


entry: 3.4.22.32
name: --- - stem bromelain - bromelain - pineapple stem bromelain
comment:
The most abundant of the cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Distinct from the bromelain found in the pineapple fruit (EC 3.4.22.33). Scarcely inhibited by chicken cystatin and also very slowly inactivated by E-64. In peptidase family C1 (papain family). Formerly EC 3.4.4.24 and included in EC 3.4.22.4

reaction:
Broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-|-NHMec amongst small molecule substrates


entry: 3.4.22.33
name:
--- 
- fruit bromelain
- juice bromelain
- ananase
- bromelase
- bromelin
- extranase
- pinase
- pineapple enzyme
- traumanase
- fruit bromelain FA2

comment:
From the pineapple plant, Ananas comosus. Scarcely inhibited by chicken cystatin. Another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain (formerly EC 3.4.99.18), is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin [4]. In peptidase family C1 (papain family). Formerly EC 3.4.22.5 and included in EC 3.4.22.4

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg-|-NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-NHMec (c.f. stem bromelain)


entry: 3.4.22.34
reaction: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds
name:
--- 
- legumain
- asparaginyl endopeptidase
- citvac
- proteinase B (ambiguous)
- hemoglobinase (ambiguous)
- PRSC1 gene product (Homo sapiens)
- vicilin peptidohydrolase
- bean endopeptidase

comment:
Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13


entry: 3.4.22.35
comment: From the protozoan, Entamoeba histolytica. In peptidase family C1 (papain family)
name:
--- 
- histolysain
- histolysin
- Entamoeba histolytica cysteine proteinase
- amebapain
- Entamoeba histolytica cysteine protease
- Entamoeba histolytica neutral thiol proteinase

reaction:
Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|- in small molecule substrates including Z-Arg-Arg-|-NHMec


entry: 3.4.22.36
name:
--- 
- caspase-1
- interleukin 1beta-converting enzyme
- protease VII
- protease A
- interleukin 1beta precursor proteinase
- interleukin 1 converting enzyme
- interleukin 1beta-converting endopeptidase
- interleukin-1beta convertase
- interleukin-1beta converting enzyme
- interleukin-1beta precursor proteinase
- prointerleukin 1beta protease
- precursor interleukin-1beta converting enzyme
- pro-interleukin 1beta proteinase
- ICE

comment:
From mammalian monocytes. Inhibited by Ac-Tyr-Val-Ala-Asp-CHN2. Type example of peptidase family C14

reaction:
Release of interleukin 1beta by specific cleavage at -Asp116-|-Ala- and -Asp27-|-Gly- bonds in precursor. Also hydrolyses the small-molecule substrate, Ac-Tyr-Val-Ala-Asp-|-NHMec


entry: 3.4.22.37
reaction: Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
name:
--- 
- gingipain R
- Arg-gingipain
- gingipain-1
- argingipain
- Arg-gingivain-55 proteinase
- Arg-gingivain-70 proteinase
- Arg-gingivain-75 proteinase
- arginine-specific cysteine protease
- arginine-specific gingipain
- arginine-specific gingivain
- RGP-1
- RGP

comment:
A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine [1], and stabilized by Ca2+. Precursor molecule contains a haemagglutinin domain [2,3]. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of family C25


entry: 3.4.22.38
name:
--- 
- cathepsin K
- cathepsin O and cathepsin X (both misleading, having been used for other enzymes)
- cathepsin O2

comment:
Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption. In peptidase family C1 (papain family)

reaction:
Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg


entry: 3.4.22.39
name: --- - adenain
comment:
A cysteine endopeptidase from adenoviruses, the type example of peptidase family C5, with a protein fold unlike that known for any other peptidase [2]. Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site [1]

reaction:
Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)


entry: 3.4.22.40
name: --- - bleomycin hydrolase - aminopeptidase C (Lactococcus lactis) [4]
comment:
The molecule is a homohexamer in which the monomers have a papain-like tertiary structure (in peptidase family C1). The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain [3]. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Known from bacteria as well as eukaryotic organisms. Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyses Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates [2]

reaction:
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred [1]


