# enzymes

entry: 3.4.22.41
name: --- - cathepsin F
comment:
Cathepsin F is a lysosomal cysteine endopeptidase of family C1 (papain family), most active at pH 5.9. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Cathepsin F is expressed in most tissues of human, mouse and rat. Human gene locus: 11q13.1-13.3

reaction:
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L


entry: 3.4.22.42
name: --- - cathepsin O
comment:
Cathepsin O is a lysosomal cysteine peptidase of family C1 (papain family). The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64. Cathepsin O is ubiquitously expressed in human tissues and the human gene locus is 4q31-32

reaction:
The recombinant human enzyme hydrolyses synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec


entry: 3.4.22.43
name: --- - cathepsin V - Cathepsin L2 - cathepsin U
comment:
Cathepsin V is a human lysosomal cysteine endopeptidase of family C1 (papain family) that is maximally active at pH 5.7 and unstable at neutral pH. Compound E-64, leupeptin and chicken cystatin are inhibitors. Human cathepsin V shows expression restricted to thymus, testis, corneal epithelium and some colon and breast carcinomas. Human gene locus: 9q22.2

reaction:
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)


entry: 3.4.22.44
name: --- - nuclear-inclusion-a endopeptidase - potyvirus NIa protease
comment:
The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei; protein a of the inclusion bodies is the endopeptidase. The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage. It is also reported that transgenic plants expressing the enzyme are resistant to viral infection. Type example of peptidase family C4.

reaction:
Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.


entry: 3.4.22.45
name: --- - helper-component proteinase - HC-Pro
comment:
Known from many potyviruses. The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities: the N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. Type example of peptidase family C6.

reaction:
Hydrolyses a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein


entry: 3.4.22.46
name: --- - L-peptidase
comment:
Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses. Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue. The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory. Type example of peptidase family C28.

reaction:
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-


entry: 3.4.22.47
name: --- - gingipain K - Lys-gingipain - PrtP proteinase
reaction: Endopeptidase with strict specificity for lysyl bonds
comment:
Activity is stimulated by glycine. Known from the bacterium Porphyromonas gingivalis and contributes to the pathogenicity of the organism. In peptidase family C25.


entry: 3.4.22.48
name: --- - staphopain - staphylopain
comment: Known from species of Staphylococcus. Type example of peptidase family C47.
reaction:
Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate


entry: 3.4.22.49
name: --- - separase - separin
comment:
In both budding yeast and human cells, cleavage of the cohesin subunit Scc1 by separase is required for sister chromatid separation in mitosis. Budding yeast separase is also known to cleave the Rec8 subunit of a meiotic cohesin complex and the kinetochore protein Slk19. Type example of peptidase family C50.

reaction:
All bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage


entry: 3.4.22.50
reaction: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B
name:
--- 
- V-cath endopeptidase
- AcNPV protease
- BmNPV protease
- NPV protease
- baculovirus cathepsin
- nucleopolyhedrosis virus protease
- viral cathepsin

comment:
In peptidase family C1. Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.


entry: 3.4.22.51
name: --- - cruzipain - congopain - cruzain - evansain - trypanopain
reaction: Broad endopeptidase specificity similar to that of cathepsin L
comment:
In peptidase family C1. Is located in the digestive vacuoles of the parasitic trypanosome and contributes to the nutrition of the organism by digestion of host proteins.


entry: 3.4.22.52
name: --- - calpain-1 - mu-calpain - calcium-activated neutral protease I
reaction: Broad endopeptidase specificity
comment:
In peptidase family C2. Requires Ca2+ at micromolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53, calpain-2.


entry: 3.4.22.53
name: --- - calpain-2 - calcium-activated neutral protease II - m-calpain - milli-calpain
reaction: Broad endopeptidase specificity
comment:
Type example of peptidase family C2. Requires Ca2+ at millimolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52, calpain-1.


entry: 3.4.23.1
name:
--- 
- pepsin A
- pepsin
- lactated pepsin
- pepsin fortior
- fundus-pepsin
- elixir lactate of pepsin
- P I
- lactated pepsin elixir
- P II
- pepsin R
- pepsin D

comment:
The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. Human pepsin A occurs in five molecular forms. Pig pepsin D [1,2] is unphosphorylated pepsin A. Type example of peptidase family A1. Formerly EC 3.4.4.1

reaction:
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-|-Val, Gln4-|-His, Glu13-|-Ala, Ala14-|-Leu, Leu15-|-Tyr, Tyr16-|-Leu, Gly23-|-Phe, Phe24-|-Phe and Phe25-|-Tyr bonds in the B chain of insulin


entry: 3.4.23.2
name: --- - pepsin B - parapepsin I - pig gelatinase
comment: Formed from pig pepsinogen B. In peptidase family A1 (pepsin A family)
reaction:
Degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe


entry: 3.4.23.3
name: --- - gastricsin - pepsin C - pig parapepsin II - parapepsin II
comment:
Formed from progastricsin, apparently in the gastric juice of most vertebrates. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Seminal plasma contains a zymogen that is immunologically identical with progastricsin [6]. In peptidase family A1 (pepsin A family). Formerly EC 3.4.4.22

reaction:
More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|- bonds. High activity on hemoglobin


entry: 3.4.23.4
name: --- - chymosin - rennin (but this should be avoided since it leads to confusion with renin)
comment:
Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Found among mammals with postnatal uptake of immunoglobulins. In peptidase family A1(pepsin A family)

reaction:
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single Ser-Phe105-|-Met-Ala bond in kappa-chain of casein


entry: 3.4.23.5
name: --- - cathepsin D
comment:
Occurs intracellularly, in lysosomes. A zymogen form is known [4]. In peptidase family A1 (pepsin A family). Formerly EC 3.4.4.23

reaction:
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin


entry: 3.4.23.6
name:
--- 
- Transferred to 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.27, 3.4.23.28 and 3.4.23.30

comment:
Transferred entry: now EC 3.4.23.18 - aspergillopepsin I; EC 3.4.23.19 - aspergillopepsin II; EC 3.4.23.20 - penicillopepsin; EC 3.4.23.21 - rhizopuspepsin; EC 3.4.23.22 - endothiapepsin; EC 3.4.23.23 - mucorpepsin; EC 3.4.23.24 - candidapepsin; EC 3.4.23.25 - saccharopepsin; EC 3.4.23.26 - rhodotorulapepsin; EC 3.4.23.27 - physaropepsin; EC 3.4.23.28 - acrocylindropepsin; EC 3.4.23.30 - pycnoporopepsin (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981, deleted 1992 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978])


entry: 3.4.23.7
name: --- - Transferred to 3.4.23.20
comment:
Transferred entry: now EC 3.4.23.20 - penicillopepsin (EC 3.4.23.7 created 1972, modified 1981, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.23.8
name: --- - Transferred to 3.4.23.25
comment:
Transferred entry: now EC 3.4.23.25 - saccharopepsin (EC 3.4.23.8 created 1972, modified 1981, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.23.9
name: --- - Transferred to 3.4.23.21
comment:
Transferred entry: now EC 3.4.23.21 - rhizopuspepsin (EC 3.4.23.9 created 1972, modified 1981, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.23.10
name: --- - Transferred to 3.4.23.22
comment:
Transferred entry: now EC 3.4.23.22 - endothiapepsin (EC 3.4.23.10 created 1972, modified 1981, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.23.12
reaction: Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg
name:
--- 
- nepenthesin
- Nepenthes aspartic proteinase
- Nepenthes acid proteinase
- nepenthacin
- nepenthasin
- aspartyl endopeptidase

comment:
From the insectivorous plants Nepenthes spp. (secretions) and Drosera peltata (ground-up leaves). Formerly EC 3.4.99.4. Aspartic endopeptidases are probably present in many other plants, including Lotus [3] (formerly EC 3.4.23.13) and sorghum [2] (formerly EC 3.4.23.14). In peptidase family A1 (pepsin A family)


entry: 3.4.23.15
name: --- - renin - angiotensin-forming enzyme - angiotensinogenase
reaction: Cleavage of Leu-|- bond in angiotensinogen to generate angiotensin I
comment:
Formed from prorenin in plasma and kidney. In peptidase family A1 (pepsin A family). Formerly EC 3.4.99.19


entry: 3.4.23.16
reaction: Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
name:
--- 
- HIV-1 retropepsin
- human immunodeficiency virus type 1 protease
- gag protease
- HIV aspartyl protease
- HIV proteinase
- retroproteinase
- HIV-1 protease
- HIV-2 protease

comment:
Present in human immunodeficiency virus type 1. Contributes to the maturation of the viral particle, and is a target of antiviral drugs. Active enzyme is a dimer of identical 11-kDa subunits. Similar enzymes occur in other retroviruses [1]. Type example of peptidase family A2


entry: 3.4.23.17
name:
--- 
- pro-opiomelanocortin converting enzyme
- prohormone converting enzyme
- pro-opiomelanocortin-converting enzyme
- proopiomelanocortin proteinase
- PCE

comment:
A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle. Formerly EC 3.4.99.38

reaction:
Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side


entry: 3.4.23.18
name:
--- 
- aspergillopepsin I
- Aspergillus acid protease
- Aspergillus acid proteinase
- Aspergillus aspartic proteinase
- Aspergillus awamori acid proteinase
- Aspergillus carboxyl proteinase
- (see also Comments)
- carboxyl proteinase
- Aspergillus kawachii aspartic proteinase
- Aspergillus saitoi acid proteinase
- pepsin-type aspartic proteinase
- Aspergillus niger acid proteinase
- sumizyme AP
- proctase P
- denapsin
- denapsin XP 271
- proctase

comment:
Found in a variety of Aspergillus species (imperfect fungi): Aspergillus awamori (awamorin, aspergillopepsin A: [8]), A. foetidus (aspergillopepsin F: [6]), A. fumigatus [7], A. kawachii [9], A. niger (proteinase B, proctase B: [2,4]), A. oryzae (trypsinogen kinase: [3,10]), A. saitoi (aspergillopeptidase A: [10]), and A. sojae [5,10]. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6

reaction:
Hydrolysis of proteins with broad specificity. Generally favours hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk


entry: 3.4.23.19
reaction: Preferential cleavage in B chain of insulin: Asn3-|-Gln, Gly13-|-Ala, Tyr26-|-Thr
name:
--- 
- aspergillopepsin II
- proteinase A
- proctase A
- Aspergillus niger var. macrosporus aspartic proteinase

comment:
Isolated from Aspergillus niger var. macrosporus, distinct from proteinase B (see aspergillopepsin I) in specificity and insensitivity to pepstatin. In peptidase family A4 (scytalidopepsin B family). Formerly included in EC 3.4.23.6


entry: 3.4.23.20
name:
--- 
- penicillopepsin
- peptidase A
- Penicillium janthinellum aspartic proteinase
- acid protease A
- Penicillium citrinum acid proteinase
- Penicillium cyclopium acid proteinase
- Penicillium expansum acid proteinase
- Penicillium janthinellum acid proteinase
- Penicillium expansum aspartic proteinase
- Penicillium aspartic proteinase
- Penicillium caseicolum aspartic proteinase
- Penicillium roqueforti acid proteinase
- Penicillium duponti aspartic proteinase
- Penicillium citrinum aspartic proteinase

comment:
From the imperfect fungus Penicillium janthinellum. In peptidase family A1 (pepsin A family). Closely related enzymes have been isolated from P. roqueforti [2] and P. duponti [3]. Formerly EC 3.4.23.7, and included in EC 3.4.23.6

reaction:
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-|-Glu in the B chain of insulin. Clots milk, and activates trypsinogen


entry: 3.4.23.21
name:
--- 
- rhizopuspepsin
- Rhizopus aspartic proteinase
- neurase
- Rhizopus acid protease
- Rhizopus acid proteinase

comment:
From the zygomycete fungus Rhizopus chinensis. A similar endopeptidase is found in R. niveus [2]. In peptidase family A1 (pepsin A family). Formerly EC 3.4.23.9, and included in EC 3.4.23.6

reaction:
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave Gln4-His, but does cleave His10-|-Leu and Val12-|-Glu in B chain of insulin


entry: 3.4.23.22
name:
--- 
- endothiapepsin
- Endothia aspartic proteinase
- Endothia acid proteinase
- Endothia parasitica acid proteinase
- Endothia parasitica aspartic proteinase

comment:
From the ascomycete Endothia parasitica. In peptidase family A1 (pepsin A family). Formerly EC 3.4.23.10, and included in EC 3.4.23.6

reaction:
Hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk


entry: 3.4.23.23
name:
--- 
- mucorpepsin
- Mucor rennin
- Mucor aspartic proteinase
- Mucor acid proteinase
- Mucor acid protease
- Mucor miehei aspartic proteinase
- Mucor miehei aspartic protease
- Mucor pusillus emporase
- Fromase 100
- Mucor pusillus rennin
- Fromase 46TL
- Mucor miehei rennin

comment:
Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6

reaction:
Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen


entry: 3.4.23.24
name:
--- 
- candidapepsin
- Candida albicans aspartic proteinase
- Candida albicans carboxyl proteinase
- Candida albicans secretory acid proteinase
- Candida olea acid proteinase
- Candida aspartic proteinase
- Candida olea aspartic proteinase

comment:
This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6

reaction:
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin


entry: 3.4.23.25
name:
--- 
- saccharopepsin
- yeast endopeptidase A
- Saccharomyces aspartic proteinase
- aspartic proteinase yscA
- proteinase A
- proteinase yscA
- yeast proteinase A
- Saccharomyces cerevisiae aspartic proteinase A
- PRA

comment:
Located in the vacuole of the baker's yeast (Saccharomyces cerevisiae) cell. In peptidase family A1 (pepsin A family). Formerly EC 3.4.23.8, and included in EC 3.4.23.6

reaction:
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg


entry: 3.4.23.26
reaction: Specificity similar to that of pepsin A. Cleaves Z-Lys-|-Ala-Ala-Ala and activates trypsinogen
name:
--- 
- rhodotorulapepsin
- Rhodotorula aspartic proteinase
- Cladosporium acid protease
- Cladosporium acid proteinase
- Paecilomyces proteinase
- Cladosporium aspartic proteinase
- Rhodotorula glutinis aspartic proteinase
- Rhodotorula glutinis acid proteinase
- Rhodotorula glutinis aspartic proteinase II
- Rhodotorula acid proteinase

comment:
From the imperfect yeast Rhodotorula glutinis. Formerly included in EC 3.4.23.6. Somewhat similar enzymes have been isolated from the imperfect yeast-like organism Cladosporium sp. [4,6] and the imperfect fungus Paecilomyces varioti ([1,2], formerly EC 3.4.99.15)


entry: 3.4.23.27
name: --- - Transferred to 3.4.21.103
comment:
Transferred entry: now EC 3.4.21.103, physarolisin (EC 3.4.23.27 created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992), deleted 2003)


entry: 3.4.23.28
name: --- - acrocylindropepsin - Acrocylindrium proteinase - Acrocylindrium acid proteinase
comment:
From the imperfect fungus Acrocylindrium sp. Has a very low pH optimum on casein of 2.0. In peptidase family A1 (pepsin A family). Formerly EC 3.4.99.1 and included in EC 3.4.23.6

reaction:
Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-|-Cys(SO3H), Glu21-|-Arg and Asn3-|-Gln, although not Gln4-His


entry: 3.4.23.29
name:
--- 
- polyporopepsin
- Polyporus aspartic proteinase
- Irpex lacteus aspartic proteinase
- Irpex lacteus carboxyl proteinase B

comment:
From the basidiomycete Polyporus tulipiferae (formerly Irpex lacteus). In peptidase family A1 (pepsin A family)

reaction:
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain


entry: 3.4.23.30
name:
--- 
- pycnoporopepsin
- proteinase Ia
- Pycnoporus coccineus aspartic proteinase
- Trametes acid proteinase

comment:
From the basidiomycete Pycnoporus sanguineus, formerly known as P. coccineus and Trametes sanguinea. Formerly included in EC 3.4.23.6

reaction:
Similar to pepsin A, but narrower, cleaving only three bonds in the B chain of insulin: Ala14-|-Leu, Tyr16-|-Leu, and Phe24-|-Phe


entry: 3.4.23.31
name:
--- 
- scytalidopepsin A
- Scytalidium aspartic proteinase A
- Scytalidium lignicolum aspartic proteinase
- Scytalidium lignicolum aspartic proteinase A-2
- Scytalidium lignicolum aspartic proteinase A-I
- Scytalidium lignicolum aspartic proteinase C
- Scytalidium lignicolum carboxyl proteinase
- Scytalidium lignicolum acid proteinase

comment:
Isolated from the imperfect fungus Scytalidium lignicolum. Not inhibited by pepstatin-Ac, methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenyl)propane. A related enzyme from the same organism, proteinase C, is also insensitive to these inhibitors and has M(r) = 406,000 [3]

reaction:
Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves Cys(SO3H)7-|-Gly and Leu17-|-Val in the B chain of insulin


entry: 3.4.23.32
name:
--- 
- scytalidopepsin B
- Scytalidium aspartic proteinase B
- Ganoderma lucidum carboxyl proteinase
- Ganoderma lucidum aspartic proteinase
- Scytalidium lignicolum aspartic proteinase B
- SLB

comment:
A second endopeptidase from Scytalidium lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate. 1,2-Epoxy-3-(p-nitrophenoxy)propane reacts with Glu53, which replaces one of the aspartic residues at the active centre. One of the smallest aspartic endopeptidases active as the monomer, with M(r) 22,000. Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes [1] and Ganoderma lucidum [3], and in Polyporus tulipiferae [4], a second endopeptidase distinct from polyporopepsin, but these are of typical aspartic endopeptidase size, M(r) about 36,000. Type example of peptidase family G1

reaction:
Hydrolysis of proteins with broad specificity, cleaving Phe24-|-Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin


entry: 3.4.23.34
reaction: Similar to cathepsin D, but slightly broader specificity
name:
--- 
- cathepsin E
- slow-moving proteinase
- erythrocyte membrane aspartic proteinase
- SMP
- EMAP
- non-pepsin proteinase
- cathepsin D-like acid proteinase
- cathepsin E-like acid proteinase
- cathepsin D-type proteinase

comment:
Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family)


entry: 3.4.23.35
name: --- - barrierpepsin - barrier proteinase - Bar proteinase
reaction: Selective cleavage of -Leu6-|-Lys- bond in the pheromone alpha-mating factor
comment:
A secreted endopeptidase known from baker's yeast (Saccharomyces cerevisiae). In peptidase family A1 (pepsin A family)


entry: 3.4.23.36
name:
--- 
- signal peptidase II
- premurein-leader peptidase
- prolipoprotein signal peptidase
- leader peptidase II
- premurein leader proteinase

comment:
An 18-kDa enzyme present in bacterial inner membranes. Inhibited by pepstatin and the antibiotic globomycin. Type example of peptidase family A8. Formerly EC 3.4.99.35

reaction:
Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein. Hydrolyses -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral sidechains


entry: 3.4.23.38
name: --- - plasmepsin I - aspartic hemoglobinase I - PFAPG - malaria aspartic hemoglobinase
comment:
Known from the malaria organism, Plasmodium. About 37 kDa. In peptidase family A1 (pepsin A family), closest to cathepsin D and renin in structure. Inhibited by pepstatin. Formerly included in EC 3.4.23.6

reaction:
Hydrolysis of the -Phe33-|-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule


entry: 3.4.23.39
name: --- - plasmepsin II - aspartic hemoglobinase II - PFAPD
comment:
Known from the malaria organism, Plasmodium. About 37 kDa. In peptidase family A1 (pepsin A family), and is 73% identical in sequence to plasmepsin I. Inhibited by pepstatin. Formerly included in EC 3.4.23.6

reaction:
Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr [3]


entry: 3.4.23.40
name: --- - phytepsin
comment:
Known particularly from barley grain, but present in other plants also. In peptidase family A1 (pepsin A family), but structurally distinct in containing an internal region of about 100 amino acids not generally present in the family

reaction:
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds


entry: 3.4.23.41
name: --- - yapsin 1 - yeast aspartic protease 3 - Yap3 gene product (Saccharomyces cerevisiae)
comment:
In peptidase family A1 of pepsin, and weakly inhibited by pepstatin. Can partially substitute for kexin in a deficient strain of yeast. The homologous product of the Mkc7 gene (Saccharomyces cerevisiae) has similar catalytic activity and has been termed yapsin 2 [2]

reaction:
Hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions


entry: 3.4.23.42
name: --- - thermopsin
reaction: Similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
comment:
From the thermophilic archeaon Sulfolobus acidocaldarius. Maximally active at pH 2 and 90 degC. Weakly inhibited by pepstatin but shows no sequence similarity to pepsin. Type example of peptidase family A5. Formerly EC 3.4.99.44


entry: 3.4.23.43
name: --- - prepilin peptidase
comment:
Many species of bacteria carry pili on their cell surfaces. These are virulence determinants in pathogenic strains, and are assembled biosynthetically from type IV prepilin subunits. Before assembly, the prepilin molecules require proteolytic processing, which is done by the prepilin peptidase. Prepilin peptidase and its homologues play a central role not only in type IV pilus biogenesis but also in transport of macromolecules across cell membranes. Although both peptide-bond hydrolysis and N-methylation are catalysed by the same molecule, the methylation can be inhibited without affecting peptidase activity, and it is believed that the enzyme has two separate catalytic sites. Type example of peptidase family A24.

reaction:
Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine


entry: 3.4.23.44
name:
--- 
- nodavirus endopeptidase
- Black Beetle virus endopeptidase
- Flock House virus endopeptidase

comment:
A single aspartic residue is critical for activity, and inhibition by EDTA indicates that a metal ion is also important. The enzyme is known from several nodaviruses that are pathogens of insects. Type example of peptidase family A6, and structurally related to the tetravirus endopeptidase in family A21, although in that family, the catalytic residue is thought to be Glu.

reaction:
Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-


entry: 3.4.23.45
name:
--- 
- memapsin 1
- beta-secretase
- beta-site Alzheimer's amyloid precursor protein cleaving enzyme 2 (BACE2)
- ASP1
- Down region aspartic protease

comment:
Can cleave beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease, but is not significantly expressed in human brain. In peptidase family A1, but is atypical in containing a C-terminal membrane-spanning domain.

reaction:
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein


entry: 3.4.23.46
name:
--- 
- memapsin 2
- beta-secretase
- beta-site Alzheimer's amyloid precursor protein cleaving enzyme 1 (BACE1)

comment:
Suggested to be the major "beta-secretase" responsible for the cleavage of the beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease. In peptidase family A1 but is atypical in containing a C-terminal membrane-spanning domain.

reaction:
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein


entry: 3.4.23.47
name: --- - HIV-2 retropepsin
reaction: Endopeptidase for which the P1 residue is preferably hydrophobic
comment:
In peptidase family A2. Responsible for the post-translational processing of the human immunodeficiency virus polyprotein.


entry: 3.4.23.48
name: --- - plasminogen activator Pla
comment: In peptidase family A26. From the bacterium Yersinia pestis that causes plague.
reaction:
Converts human Glu-plasminogen to plasmin by cleaving the Arg560-|-Val peptide bond that is also hydrolysed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins


entry: 3.4.23.49
name:
--- 
- omptin
- protease VII
- protease A
- gene ompT proteins
- ompT protease
- protein a
- Pla
- OmpT

comment:
A product of the ompT gene of Escherichia coli, and associated with the outer membrane. Omptin shows a preference for cleavage between consecutive basic amino acids, but is capable of cleavage when P1' is a non-basic residue [5,7]. Belongs in peptidase family A26.

reaction:
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.


entry: 3.4.24.1
name:
--- 
- atrolysin A
- Crotalus atrox metalloendopeptidase a
- hemorrhagic toxin a
- Crotalus atrox alpha-proteinase
- Crotalus atrox proteinase
- bothropasin

comment:
A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins in the venom of western diamondback rattlesnake. The 60 kDa hemorrhagic toxin 1 of Crotalus ruber ruber shows identical specificity [2]. In peptidase family M12 (astacin family). Related metalloendopeptidases from rattlesnake venoms are EC 3.4.24.41 (atrolysin B), EC 3.4.24.42 (atrolysin C), EC 3.4.24.43 (atroxase), EC 3.4.24.44 (atrolysin E), EC 3.4.24.45 (atrolysin F), EC 3.4.24.46 (adamalysin), EC 3.4.24.47 (horrilysin), and EC 3.4.24.48 (ruberlysin)

reaction:
Cleavage of Asn3-|-Gln, His5-|-Leu, His10-|-Leu, Ala14-|-Leu and Tyr16-|-Leu in insulin B chain; removes C-terminal Leu from small peptides


entry: 3.4.24.3
name:
--- 
- microbial collagenase
- Clostridium histolyticum collagenase
- clostridiopeptidase A
- collagenase A
- collagenase I
- Achromobacter iophagus collagenase
- collagenase
- aspergillopeptidase C
- nucleolysin
- azocollase
- metallocollagenase
- soycollagestin
- Clostridium histolyticum proteinase A
- clostridiopeptidase II
- MMP-8
- clostridiopeptidase I
- collagen peptidase
- collagen protease
- collagenase MMP-1
- metalloproteinase-1
- kollaza
- matrix metalloproteinase-1
- MMP-1
- matrix metalloproteinase-8
- matirx metalloproteinase-18
- interstitial collagenase

comment:
Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus [10], Empedobacter collagenolyticum [4], Pseudomonas marinoglutinosa [1], and species of Vibrio, Vibrio B-30 (ATCC 21250) [2] and V. alginolyticus (previously Achromobacter iophagus) [3,8]. Also known from Streptomyces sp. [9]. The Vibrio enzyme is the type example of peptidase family M9. Formerly EC 3.4.99.5, EC 3.4.4.19 and EC 3.4.24.8

reaction:
Digestion of native collagen in the triple helical region at -|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1'; Pro and Ala at P2 and P2'; and hydroxyproline, Ala or Arg at P3'


entry: 3.4.24.4
name:
--- 
- Transferred to 3.4.24.25, 3.4.24.26, 3.4.24.27, 3.4.24.28, 3.4.24.29, 3.4.24.30, 3.4.24.31, 3.4.24.32, 3.4.24.39 and 3.4.24.40

comment:
Transferred entry: now EC 3.4.24.25 - aeromonolysin, EC 3.4.24.26 - pseudolysin, EC 3.4.24.27 - thermolysin, EC 3.4.24.28 - bacillolysin, EC 3.4.24.29 - aureolysin, EC 3.4.24.30 - coccolysin, EC 3.4.24.31 - mycolysin, EC 3.4.24.32 - beta-lytic metalloendopeptidase, EC 3.4.24.39 - deuterolysin, EC 3.4.24.40 - serralysin (EC 3.4.24.4 created 1972 [EC 3.4.99.13 and EC 3.4.99.22 both created 1972, incorporated 1978], deleted 1992)


entry: 3.4.24.5
name: --- - Deleted entry
comment:
Deleted entry: lens neutral proteinase. Now included with EC 3.4.22.17 - calpain and EC 3.4.99.46 - multicatalytic endopeptidase complex (EC 3.4.24.5 created 1978, deleted 1989)


entry: 3.4.24.6
name: --- - leucolysin - Leucostoma neutral proteinase - Leucostoma peptidase A
comment: From the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma).
reaction:
Cleavage of Phe1-|-Val, His5-|-Leu, Ala14-|-Leu, Gly20-|-Glu, Gly23-|-Phe and Phe24-|-Phe bonds in insulin B chain as well as N-blocked dipeptides


entry: 3.4.24.7
name: --- - interstitial collagenase - vertebrate collagenase - matrix metalloproteinase 1
comment:
The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain. However, alpha-macroglobulins are cleaved much more rapidly. The enzyme is widely distributed in vertebrate animals. Type example of peptidase family M10

reaction:
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-|-Ile in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue


entry: 3.4.24.8
name: --- - Transferred to 3.4.24.3
comment:
Transferred entry: now included with EC 3.4.24.3 - microbial collagenase (EC 3.4.24.8 created 1978, deleted 1992)


entry: 3.4.24.10
name: --- - Deleted entry
comment:
Deleted entry: Trichophyton mentagrophytes keratinase (EC 3.4.24.10 created 1972 as EC 3.4.99.12, transferred 1978 to EC 3.4.24.10, deleted 1992)


entry: 3.4.24.11
name:
--- 
- neprilysin
- neutral endopeptidase
- endopeptidase 24.11
- kidney-brush-border neutral peptidase
- enkephalinase (misleading)
- endopeptidase-2
- CALLA (common acute lymphoblastic leukemia-associated) antigens
- CALLA antigen
- endopeptidase
- membrane metalloendopeptidase
- kidney-brush-border neutral endopeptidase
- kidney-brush-border neutral proteinase
- CALLA glycoprotein
- CALLA
- common acute lymphoblastic leukemia antigen
- CALLA glycoproteins
- common acute lymphoblastic leukemia-associated antigens
- neutral metallendopeptidase
- NEP
- neutral endopeptidase 24.11
- CD10
- acute lymphoblastic leukemia antigen

comment:
A membrane-bound glycoprotein widely distributed in animal tissues. Inhibited by phosphoramidon and thiorphan. Common acute lymphoblastic leukemia antigen (CALLA). Type example of peptidase family M13

reaction:
Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'


entry: 3.4.24.12
reaction: Hydrolysis of proteins of the fertilization envelope and dimethylcasein
name:
--- 
- envelysin
- sea-urchin-hatching proteinase
- hatching enzyme
- chorionase
- chorion-digesting proteinase
- chymostrypsin
- sea urchin embryo hatching enzyme

comment:
A glycoprotein from various members of the class Echinoidea. Extracellular enzyme requiring Ca2+. In peptidase family M10 (interstitial collagenase family)


entry: 3.4.24.13
reaction: Cleavage of Pro-|-Thr bond in the hinge region of the heavy chain of human IgA
name:
--- 
- IgA-specific metalloendopeptidase
- immunoglobulin A1 proteinase
- IgA protease
- IgA1-specific proteinase
- IgA1 protease
- IgA1 proteinase

comment:
A 190 kDa enzyme found in several pathogenic species of Streptococcus such as sanguis and pneumoniae. Type example of peptidase family M26. There is also an IgA-specific prolyl endopeptidase of the serine-type (see EC 3.4.21.72, IgA-specific serine endopeptidase)


entry: 3.4.24.14
name:
--- 
- procollagen N-endopeptidase
- procollagen N-terminal peptidase
- procollagen aminopeptidase
- aminoprocollagen peptidase
- aminoterminal procollagen peptidase
- procollagen aminoterminal protease
- procollagen N-terminal proteinase
- type I/II procollagen N-proteinase
- type III procollagen

comment:
Removes the propeptides of type I and II collagens prior to fibril assembly. Does not act on type III collagen. In peptidase family M12 (astacin family)

reaction:
Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln


entry: 3.4.24.15
name:
--- 
- thimet oligopeptidase
- Pz-peptidase
- soluble metalloendopeptidase
- endo-oligopeptidase A
- tissue-endopeptidase degrading collagenase-synthetic-substrate

comment:
Thiol compounds activate at low concentrations. Type example of peptidase family M3. Formerly also EC 3.4.22.19 and EC 3.4.99.31

reaction:
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues


entry: 3.4.24.16
reaction: Preferential cleavage in neurotensin: Pro10-|-Tyr
name:
--- 
- neurolysin
- neurotensin endopeptidase
- endopeptidase 24.16
- endo-oligopeptidase B (proline-endopeptidase)

comment:
No absolute requirement for a prolyl bond: the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do. In peptidase family M3 (thimet oligopeptidase family)


entry: 3.4.24.17
reaction: Preferential cleavage where P1', P2' and P3' are hydrophobic residues
name:
--- 
- stromelysin 1
- matrix metalloproteinase 3
- proteoglycanase
- collagenase activating protein
- procollagenase activator
- transin
- MMP-3
- neutral proteoglycanase
- stromelysin
- collagen-activating protein

comment:
An extracellular endopeptidase of vertebrate tissues homologous with interstitial collagenase. Digests proteoglycan, fibronectin, collagen types III, IV, V, IX, and activates procollagenase. In peptidase family M10 (interstitial collagenase family)


entry: 3.4.24.18
name:
--- 
- meprin A
- endopeptidase-2
- meprin-a
- meprin
- N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase
- PABA-peptide hydrolase
- PPH

comment:
A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 3.4.24.11) include insensitivity to phosphoramidon and thiorphan. PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli [4]. In peptidase family M12 (astacin family). Formerly included in EC 3.4.24.11

reaction:
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues


entry: 3.4.24.19
name:
--- 
- procollagen C-endopeptidase
- procollagen C-terminal proteinase
- carboxyprocollagen peptidase
- procollagen C-terminal peptidase
- procollagen C-proteinase
- procollagen carboxypeptidase
- procollagen carboxy-terminal proteinase
- procollagen peptidase

comment:
A 100 kDa endopeptidase the activity of which is increased by Ca2+ and by an enhancer glycoprotein. In peptidase family M12 (astacin family)

reaction:
Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III


entry: 3.4.24.20
reaction: Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro)
name:
--- 
- peptidyl-Lys metalloendopeptidase
- Armillaria mellea neutral proteinase
- peptidyllysine metalloproteinase

comment:
From the honey fungus Armillaria mellea. In peptidase family M35 (deuterolysin family). Formerly EC 3.4.99.32.


entry: 3.4.24.21
name: --- - astacin - Astacus proteinase - crayfish small-molecule proteinase
comment:
A 22.6 kDa digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis. Type example of peptidase family M12. Formerly EC 3.4.99.6

reaction:
Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'


entry: 3.4.24.22
name: --- - stromelysin 2 - matrix metalloproteinase 10 - transin 2 - proteoglycanase 2
reaction: Similar to stromelysin 1, but action on collagen types III, IV and V is weak
comment:
In peptidase family M10 (interstitial collagenase family). Digests gelatin types I, III, IV, V, fibronectin and proteoglycan


entry: 3.4.24.23
name:
--- 
- matrilysin
- matrin
- uterine metalloendopeptidase
- matrix metalloproteinase 7
- putative (or punctuated) metalloproteinase-1
- matrix metalloproteinase pump 1
- MMP 7
- PUMP-1 proteinase
- PUMP
- metalloproteinase pump-1
- putative metalloproteinase
- MMP

comment:
Found in rat uterus; at 19 kDa, the smallest member of peptidase family M10 (interstitial collagenase family). Similar in specificity to stromelysin, but more active on azocoll

reaction:
Cleavage of Ala14-|-Leu and Tyr16-|-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I)


entry: 3.4.24.24
name:
--- 
- gelatinase A
- 72-kDa gelatinase
- matrix metalloproteinase 2
- type IV collagenase
- 3/4 collagenase (Obsolete)
- matrix metalloproteinase 5 (Obsolete)
- 72 kDa gelatinase type A
- collagenase IV
- collagenase type IV
- MMP 2
- type IV collagen metalloproteinase
- type IV collagenase/gelatinase

comment:
A secreted endopeptidase in peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain

reaction:
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln


entry: 3.4.24.25
name: --- - vibriolysin - Aeromonas proteolytica neutral proteinase - aeromonolysin
comment:
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 3.4.24.4

reaction:
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin


entry: 3.4.24.26
name: --- - pseudolysin - Pseudomonas elastase - Pseudomonas aeruginosa neutral metalloproteinase
comment:
In peptidase family M4 (thermolysin family). From the pathogenic bacteria Pseudomonas aeruginosa and Legionella pneumophila, and causes tissue damage. Formerly included in EC 3.4.24.4

reaction:
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects


entry: 3.4.24.27
reaction: Preferential cleavage: -|-Leu > -|-Phe
name:
--- 
- thermolysin
- Bacillus thermoproteolyticus neutral proteinase
- thermoase
- thermoase Y10
- TLN

comment:
A thermostable extracellular metalloendopeptidase containing four calcium ions. Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus [4] and Aspergillus oryzae [5]. Formerly included in EC 3.4.24.4. Type example of peptidase family M4. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin


entry: 3.4.24.28
reaction: Similar, but not identical, to that of thermolysin
name:
--- 
- bacillolysin
- Bacillus metalloendopeptidase
- Bacillus subtilis neutral proteinase
- anilozyme P 10
- Bacillus metalloproteinase
- Bacillus neutral proteinase
- megateriopeptidase

comment:
Variants of this enzyme have been found in species of Bacillus including B. subtilis [1,6], B. amyloliquefaciens [5], B. megaterium (megateriopeptidase, [2]), B. mesentericus [10], B. cereus [3,8,9] and B. stearothermophilus [7]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4


entry: 3.4.24.29
name:
--- 
- aureolysin
- Staphylococcus aureus neutral proteinase
- Staphylococcus aureus neutral protease

comment:
A metalloenzyme from S. aureus earlier confused with staphylokinase (a non-enzymatic activator of plasminogen). Formerly EC 3.4.99.22 and included in EC 3.4.24.4

reaction:
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus


entry: 3.4.24.30
name: --- - coccolysin - Streptococcus thermophilus intracellular proteinase - EM 19000
reaction: Preferential cleavage: -|-Leu, -|-Phe, -|-Tyr, -|-Ala
comment:
A 30 kDa endopeptidase found intracellularly in S. thermophilus [1] and S. diacetilactis [2] and in the medium of S. faecalis [3,4]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4


entry: 3.4.24.31
reaction: Preferential cleavage of bonds with hydrophobic residues in P1'
name:
--- 
- mycolysin
- pronase component
- Streptomyces griseus neutral proteinase
- actinase E
- SGNPI

comment:
From Streptomyces griseus, S. naraensis, and S. cacaoi. Specificity similar to that of thermolysin, but much more sensitive to inhibition by mercaptoacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5. Formerly included in EC 3.4.24.4


entry: 3.4.24.32
reaction: Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at Gly23-|-Phe > Val18-|-Cya
name:
--- 
- beta-lytic metalloendopeptidase
- Myxobacter beta-lytic proteinase
- achromopeptidase component
- beta-lytic metalloproteinase
- beta-lytic protease
- Myxobacterium sorangium beta-lytic proteinase
- Myxobacter495 beta-lytic proteinase

comment:
From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23. Formerly EC 3.4.99.13 and included in EC 3.4.24.4.


entry: 3.4.24.33
name: --- - peptidyl-Asp metalloendopeptidase - endoproteinase Asp-N - peptidyl-Asp metalloproteinase
reaction: Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds
comment:
A metalloenzyme isolated from Pseudomonas fragi. Useful in protein sequencing applications because of its limited specificity. In peptidase family M72.


entry: 3.4.24.34
name: --- - neutrophil collagenase - matrix metalloproteinase 8 - PMNL collagenase - MMP-8
comment:
Similar to interstitial collagenase in specificity, but the product of a different gene and highly glycosylated. Stored in the specific granules of neutrophil leukocytes. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.7

reaction:
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I


entry: 3.4.24.35
reaction: Cleavage of gelatin types I and V and collagen types IV and V
name:
--- 
- gelatinase B
- 92-kDa gelatinase
- matrix metalloproteinase 9
- type V collagenase
- 92-kDa type IV collagenase
- macrophage gelatinase
- 95 kDa type IV collagenase/gelatinase
- collagenase IV
- collagenase type IV
- gelatinase MMP 9
- MMP 9
- type IV collagen metalloproteinase

comment:
Similar to gelatinase A, but possesses a further domain . In peptidase family M10 (interstitial collagenase family)


entry: 3.4.24.36
name:
--- 
- leishmanolysin
- promastigote surface endopeptidase
- glycoprotein gp63
- Leishmania metalloproteinase
- surface acid proteinase
- promastigote surface protease

comment:
A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100-|-Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8

reaction:
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-


entry: 3.4.24.37
reaction: Cleavage of Pro-|-Phe and Ala-|-Ala bonds
name:
--- 
- saccharolysin
- proteinase yscD
- yeast cysteine proteinase D (Misleading)
- Saccharomyces cerevisiae proteinase yscD

comment:
An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from Saccharomyces cerevisiae. In peptidase family M3 (thimet oligopeptidase family). Formerly EC 3.4.22.22


entry: 3.4.24.38
name:
--- 
- gametolysin
- autolysin, Chlamydomonas cell wall degrading protease
- lysin
- Chlamydomonas reinhardtii metalloproteinase
- gamete lytic enzyme
- gamete autolysin

comment:
A glycoprotein found in the periplasmic space of Chlamydomonas reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa upon activation. A zinc enzyme, inhibited by phosphoramidon, but also thiol activated. Type example of peptidase family M11

reaction:
Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala


entry: 3.4.24.39
name:
--- 
- deuterolysin
- Penicillium roqueforti protease II
- microbial neutral proteinase II
- acid metalloproteinase
- neutral proteinase II
- Penicillium roqueforti metalloproteinase

comment:
Proteolytic activity found in Penicillium roqueforti [4], P. caseicolum [4], Aspergillus sojae [3] and A. oryzae [1,5]. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4

reaction:
Preferential cleavage of bonds with hydrophobic residues in P1'; also Asn3-|-Gln and Gly8-|-Ser bonds in insulin B chain


entry: 3.4.24.40
reaction: Preferential cleavage of bonds with hydrophobic residues in P1'
name:
--- 
- serralysin
- Pseudomonas aeruginosa alkaline proteinase
- Escherichia freundii proteinase
- Serratia marcescens extracellular proteinase
- Serratia marcescens metalloproteinase
- Pseudomonas aeruginosa alk. protease
- Serratia marcescens metalloprotease

comment:
A 50 kDa extracellular endopeptidase from Pseudomonas aeruginosa [1,2,6], Escherichia freundii [3], Serratia marcescens [4,5,6] and Erwinia chrysanthemi [7]. There is broad specificity in cleavage of the insulin B chain, with some species variations. The pH optimum for digesting various proteins is about 9 - 10. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.4


entry: 3.4.24.41
name: --- - atrolysin B - Crotalus atrox metalloendopeptidase b - hemorrhagic toxin b - Ht-b
comment:
From the venom of the western diamondback rattlesnake (Crotalus atrox). In peptidase family M12 (astacin family)

reaction:
Cleavage of His5-|-Leu, His10-|-Leu, Ala14-|-Leu, Tyr16-|-Leu and Gly23-|-Phe of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves -|-Ser bonds in glucagon


entry: 3.4.24.42
name: --- - atrolysin C - Crotalus atrox metalloendopeptidase c - hemorrhagic toxin c and d
comment:
A 24 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests type IV collagen, and exists as two forms, c and d. Phosphoramidon inhibits in the 0.1 mM range. In peptidase family M12 (astacin family). Hemorrhagic toxin-2 of C. ruber ruber has the same Mr and specificity and is a homologue [4,6]

reaction:
Cleavage of His5-|-Leu, His10-|-Leu, Ala14-|-Leu, Tyr16-|-Leu and Gly23-|-Phe bonds in B chain of insulin. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1


entry: 3.4.24.43
name: --- - atroxase
reaction: Cleavage of His5-|-Leu, Ser9-|-His, His10-|-Leu, Ala14-|-Leu and Tyr16-|-Leu of insulin B chain
comment:
A nonhemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that cleaves fibrinogen. In peptidase family M12 (astacin family)


entry: 3.4.24.44
name: --- - atrolysin E - Crotalus atrox metalloendopeptidase e - hemorrhagic toxin e
comment:
A 25.7 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests basement membrane components, including the triple helix of type IV collagen. Such action is believed to contribute to the hemorrhagic property by weakening capillary walls. In peptidase family M12 (astacin family)

reaction:
Cleavage of Asn3-|-Gln, Ser9-|-His and Ala14-|-Leu bonds in insulin B chain and Tyr14-|-Gln and Thr8-|-Ser in A chain. Cleaves type IV collagen at Ala73-|-Gln in alpha1(IV) and at Gly7-|-Leu in alpha2(IV)


entry: 3.4.24.45
name:
--- 
- atrolysin F
- Crotalus atrox metalloendopeptidase
- hemorrhagic toxin f
- Crotalus atrox metalloendopeptidase f

comment:
A 64 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests the gamma chain of fibrinogen. Immunologically distinct from EC 3.4.24.1, atrolysin A.

reaction:
Cleavage of Val2-|-Asn, Gln4-|-His, Leu6-|-Cys, His10-|-Leu, Ala14-|-Leu and Tyr16-|-Leu bonds in insulin B chain


entry: 3.4.24.46
name:
--- 
- adamalysin
- Crotalus adamanteus metalloendopeptidase
- proteinase I and II
- Crotalus adamanteus venom proteinase II
- adamalysin II

comment:
From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate alpha1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family)

reaction:
Cleavage of Phe1-|-Val, His5-|-Leu, His10-|-Leu, Ala14-|-Leu, Leu15-|-Tyr, and Tyr16-|-Leu of insulin B chain


entry: 3.4.24.47
name:
--- 
- horrilysin
- Crotalus horridus metalloendopeptidase
- hemorrhagic proteinase IV
- Crotalus horridus horridus venom hemorrhagic proteinase

comment:
A 56 kDa hemorrhagic endopeptidase from the venom of the timber rattlesnake (Crotalus horridus horridus) that cleaves basement membrane, hide powder and fibrinogen.

reaction:
Cleavage of only the single bond Ala14-|-Leu in the insulin B chain, Ser12-|-Leu in the A chain, and Ile-|-Gly, Pro-|-Ala, and Ser-|-Trp in melittin


entry: 3.4.24.48
name: --- - ruberlysin - Crotalus ruber metalloendopeptidase II - hemorrhagic toxin II
comment:
A 25 kDa hemorrhagic endopeptidase from the venom of the red rattlesnake (Crotalus ruber ruber) that cleaves fibrinogen. In peptidase family M12 (astacin family)

reaction:
Cleavage of His10-|-Leu, Ala14-|-Leu, Tyr16-|-Leu and Gly23-|-Phe bonds in the B chain of insulin; His-|-Pro, Pro-|-Phe, and Trp-|-Ser of angiotensin I; and Gly-|-Phe of Met enkephalin


entry: 3.4.24.49
name: --- - bothropasin - Bothrops jararaca venom metalloproteinase
reaction: Cleavage of His5-|-Leu, His10-|-Leu, Ala14-|-Leu, Tyr16-|-Leu and Phe24-|-Phe in insulin B chain
comment:
Caseinolytic endopeptidase of jararaca snake (Bothrops jararaca) venom; 48 kDa. In peptidase family M12


entry: 3.4.24.50
name: --- - bothrolysin - Bothrops metalloendopeptidase J - J protease
comment:
A 22.5 kDa endopeptidase from the venom of the jararaca snake (Bothrops jararaca), insensitive to phosphoramidon at 0.5 mM. In peptidase family M12 (astacin family)

reaction:
Cleavage of Gln4-|-His, Ser9-|-His and Ala14-|-Leu of insulin B chain and Pro-|-Phe of angiotensin I


entry: 3.4.24.52
reaction: Cleavage of only two bonds His10-|-Leu and Ala14-|-Leu in the insulin B chain
name:
--- 
- trimerelysin I
- Trimeresurus metalloendopeptidase I
- hemorrhagic proteinase HR1A
- hemorrhagic metalloproteinase HR1A
- metalloproteinase HR1A

comment:
A 60 kDa hemorrhagic endopeptidase of pI 4.4 from the venom of the habu snake (Trimeresurus flavoviridis). In peptidase family M12 (astacin family)


entry: 3.4.24.53
name: --- - trimerelysin II - Trimeresurus metalloendopeptidase II - proteinase H2 - H2-proteinase
comment:
A 24 kDa nonhemorrhagic endopeptidase from the venom of the habu snake (Trimeresurus flavoviridis). In peptidase family M12 (astacin family)

reaction:
Cleavage of Asn3-|-Gln, His10-|-Leu and Ala14-|-Leu in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase


entry: 3.4.24.54
name: --- - mucrolysin - Trimeresurus metalloendopeptidase A - mucrotoxin A
comment:
A 94 kDa hemorrhagic and fibrinogenolytic endopeptidase from the Chinese habu snake (Trimeresurus mucrosquamatus) venom. In peptidase family M12 (astacin family)

reaction:
Cleavage of Ser9-|-His, His10-|-Leu, Ala14-|-Leu, Leu15-|-Tyr and Tyr16-|-Leu bonds in insulin B chain


entry: 3.4.24.55
name:
--- 
- pitrilysin
- Escherichia coli protease III
- protease Pi
- proteinase Pi
- PTR
- Escherichia coli metalloproteinase Pi

comment:
From the periplasmic space of Escherichia coli. Inhibited by EDTA and 1,10-phenanthroline; not thiol-dependent. Formerly EC 3.4.99.44. Type example of peptidase family M16

reaction:
Preferential cleavage of -Tyr16-|- Leu- and -Phe25-|- Tyr-bonds of oxidized insulin B chain. Also acts on other substrates of less than 7 kDa such as insulin and glucagon


entry: 3.4.24.56
reaction: Degradation of insulin, glucagon and other polypeptides. No action on proteins
name:
--- 
- insulysin
- insulinase
- insulin-degrading enzyme
- insulin protease
- insulin proteinase
- insulin-degrading neutral proteinase
- insulin-specific protease
- insulin-glucagon protease
- metalloinsulinase
- IDE

comment:
A 110 kDa cytosolic enzyme, known from mammals and the fruit fly, Drosophila melanogaster. Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. In peptidase family M16 (pitrilysin family). Formerly EC 3.4.22.11, EC 3.4.99.10 and EC 3.4.99.45


entry: 3.4.24.57
name:
--- 
- O-sialoglycoprotein endopeptidase
- glycoprotease
- glycophorin A proteinase
- glycoproteinase
- sialoglycoprotease
- sialoglycoproteinase

comment:
An enzyme secreted by the bacterium Pasteurella haemolytica. Inhibited by EDTA (100 mM) and 1,10-phenanthroline. Type example of peptidase family M22

reaction:
Hydrolysis of O-sialoglycoproteins; cleaves -Arg31-|-Asp- bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated


entry: 3.4.24.58
name:
--- 
- russellysin
- Russell's viper venom factor X activator, RVV-X
- blood-coagulation factor X activating enzyme
- metalloproteinase RVV-x
- Vipera russelli proteinase
- Russell's viper blood coagulation factor X activator
- RVV-V

comment:
This enzyme from the venom of Russell's viper (Vipera russelli) of 79 kDa comprises a heavy (59 kDa) and a heterogeneous light (18-21 kDa) chain. Contains Ca2+ and Zn2+. The heavy chain contains the zinc-binding endopeptidase domain and a disintegrin. In peptidase family M12 (astacin family)

reaction:
Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of -Arg-|- bonds. Has no action on insulin B chain


entry: 3.4.24.59
name:
--- 
- mitochondrial intermediate peptidase
- mitochondrial intermediate precursor-processing proteinase
- MIP

comment:
A homologue of thimet oligopeptidase. Natural substrates are precursor proteins that have already been processed by mitochondrial processing peptidase. In peptidase family M3 (thimet oligopeptidase family)

reaction:
Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion


entry: 3.4.24.60
name: --- - dactylysin - peptide hormone inactivating endopeptidase - PHIE
comment:
An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (Dactyletre du Cap). Resembles neprilysin in insensitivity to 1 muM captopril, but differs from it in being insensitive to thiorphan (1 muM) and unable to digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin, and substance P-(7-11)-peptide. A similar endopeptidase is found in human neuroblastoma cells [2]

reaction:
Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe-|-Phe- and -Phe-|-Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively


entry: 3.4.24.61
name: --- - nardilysin - N-arginine dibasic convertase - NRD-convertase
comment:
Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family)

reaction:
Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys


entry: 3.4.24.62
name:
--- 
- magnolysin
- bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin
- pro-oxytocin/neurophysin convertase
- prooxyphysin proteinase
- pro-oxytocin convertase

comment:
An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum [4,5]. Inhibited by EDTA [1]

reaction:
Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg-|-Ala-Val-. The specificity further depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the paired basic amino acids near the centre [3]


entry: 3.4.24.63
name: --- - meprin B - meprin-b
comment:
A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin beta subunits (in contrast to meprin A, which contains both alpha and beta subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family)

reaction:
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-|-Leu-, -Leu6-|-Cys-, -Ala14-|-Leu- and -Cys19-|-Gly- bonds in insulin B chain


entry: 3.4.24.64
name:
--- 
- mitochondrial processing peptidase
- processing enhancing peptidase (for one of two subunits)
- mitochondrial protein precursor-processing proteinase
- matrix peptidase
- matrix processing peptidase
- matrix processing proteinase
- MPP

comment:
Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin [3], and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Formerly EC 3.4.99.41

reaction:
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2


entry: 3.4.24.65
name: --- - macrophage elastase - metalloelastase - human macrophage metalloelastase (HME)
comment:
This enzyme is synthesized as a proenzyme of 53 kDa that is converted to an active form of 22 kDa. cDNA sequences have been obtained for the mouse [3] and human [4] enzymes. In peptidase family M10 (interstitial collagenase family)

reaction:
Hydrolysis of soluble and insoluble elastin [1]. Specific cleavages are also produced at -Ala14-|-Leu- and -Tyr16-|-Leu- in the B chain of insulin [2]


entry: 3.4.24.66
name: --- - choriolysin L - teleost hatching enzyme (component) - low choriolytic enzyme (LCE)
comment:
Known from the teleost fish Oryzias latipes (medaka). Efficient dissolution of the egg membrane requires concerted action with choriolysin H. A 24 kDa peptidase family M12 (astacin family)

reaction:
Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide


entry: 3.4.24.67
name: --- - choriolysin H - teleost hatching enzyme (component) - high choriolytic enzyme (HCE)
comment:
Known from the teleost fish Oryzias latipes (medaka). Efficient dissolution of the egg membrane requires concerted action with choriolysin L. A 25.5 kDa peptidase in family M12 (astacin family)

reaction:
Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide


entry: 3.4.24.68
name: --- - tentoxilysin - tetanus neurotoxin
comment:
Zinc enzyme produced by Clostridium tetani. Proenzyme of 150 kDa is processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activity. Weakly inhibited by captopril, and phosphoramidon. The clostridial neurotoxins disable the neuroexocytosis apparatus, and have been described as the most toxic substances known. Tentoxilysin acts at the spinal inhibitory interneurons, blocking the release of various neurotransmitters to produce spastic paralysis. Type example of peptidase family M27 (tentoxilysin family)

reaction:
Hydrolysis of -Gln76-|-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)


entry: 3.4.24.69
name: --- - bontoxilysin - botulinum neurotoxin - BoNT
comment:
This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus [1-5]. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family)

reaction:
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates


entry: 3.4.24.70
name: --- - oligopeptidase A - 68000-M signalpeptide hydrolase
comment:
Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase, in peptidase family M3 (thimet oligopeptidase family), but differs from thimet oligopeptidase in lack of thiol-activation

reaction:
Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)5 [4]


entry: 3.4.24.71
name: --- - endothelin-converting enzyme 1 - endothelin-converting enzyme - ECE-1
reaction: Hydrolysis of the -Trp21-|-Val- bond in big endothelin to form endothelin 1
comment:
A phosphoramidon-sensitive metalloendopeptidase in peptidase family M13 (neprilysin family). An integral membrane protein predominantly of endothelial cells, which generates the potent vasoconstrictor endothelin 1 from its inactive precursor


entry: 3.4.24.72
reaction: Hydrolysis of -Ala14-|-Leu- in insulin B chain and -Lys413-|-Leu- in Aalpha-chain of fibrinogen
name:
--- 
- fibrolase
- fibrinolytic proteinase
- Agkistrodon contortrix contortrix metalloproteinase
- Agkistrodon contortrix contortrix venom metalloproteinase

comment:
A 23-kDa, non-haemorrhagic enzyme from the venom of the southern copperhead snake (Agkistrodon contortix contortix). In peptidase family M12 (astacin family)


entry: 3.4.24.73
name: --- - jararhagin - HF2-proteinase - JF1
reaction: Hydrolysis of -His10-|-Leu-, -Ala14-|-Leu-, -Tyr16-|-Leu-and -Phe24-|-Phe- bonds in insulin B chain
comment:
Haemorrhagic endopeptidase from the venom of the jararaca snake (Bothrops jararaca). The 52-kDa enzyme contains a disintegrin domain [3]. In peptidase family M12 (astacin family)


entry: 3.4.24.74
name: --- - fragilysin - Bacteroides fragilis (entero)toxin
comment:
Thought to be a cause of diarrhoea in animals and humans. Hydrolyses extracellular matrix proteins, and disrupts tight junctions of intestinal epithelial cells. Also degrades intracellular, cytoskeletal proteins actin, myosin and others. In peptidase family M10 (interstitial collagenase family)

reaction:
Broad proteolytic specificity, bonds hydrolysed including -Gly-|-Leu-, -Met-|-Leu-, -Phe-|-Leu-, -Cys-|-Leu-, Leu-|-Gly


entry: 3.4.24.75
name: --- - lysostaphin - glycyl-glycine endopeptidase
comment:
A zinc-dependent, 25-kDa endopeptidase from Staphylococcus simulans. Lyses cells of S. aureus, in particular, by its action on the cross-bridges of the cell wall. Type example of peptidase family M23

reaction:
Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans


entry: 3.4.24.76
name: --- - flavastacin
reaction: Hydrolyses polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu
comment:
A zinc metalloendopeptidase in peptidase family M12 (astacin family), secreted by the bacterium Flavobacterium meningosepticum . The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp metalloendopeptidase from Pseudomonas fragi but the two are reported to be structurally dissimilar


entry: 3.4.24.77
name: --- - snapalysin - small neutral protease - SnpA gene product (Streptomyces lividans)
comment: Type example of peptidase family M7.
reaction:
Hydrolyses proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides


entry: 3.4.24.78
name: --- - gpr endopeptidase - germination proteinase
reaction: Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala
comment:
Initiates the degradation of small, acid-soluble proteins during spore germination in Bacillus megaterium. Type example of peptidase family M63.


entry: 3.4.24.79
name:
--- 
- pappalysin-1
- insulin-like growth factor binding protein-4 protease
- pregnancy-associated plasma protein-A

comment:
A 400-kDa disulfide-linked dimer. Circulates in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor of the peptidase. The rate of hydrolysis of IGFBP-4 is increased about 20-fold by the presence of insulin-like growth factor (IGF), whereas that of IGFBP-5 is decreased about two-fold. In peptidase family M43.

reaction:
Cleavage of the Met135-|-Lys bond in insulin-like growth factor binding protein (IGFBP)-4, and the Ser143-|-Lys bond in IGFBP-5


entry: 3.4.24.80
name: --- - membrane-type matrix metalloproteinase-1 - matrix metalloproteinase 14
comment:
In peptidase family M10, but, unlike most members of the family, is membrane-anchored. Believed to play an important role in the activation of progelatinase A at cell surfaces.

reaction:
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-|-Leu. Other bonds hydrolysed include Gly35-|-Ile in the propeptide of collagenase 3, and Asn341-|-Phe, Asp441-|-Leu and Gln354-|-Thr in the aggrecan interglobular domain


entry: 3.4.24.81
name: --- - ADAM10 endopeptidase - Kuzbanian protein - myelin-associated disintegrin metalloproteinase
reaction: Endopeptidase of broad specificity
comment:
In peptidase family M12. Partially responsible for the "alpha-secretase" activity in brain that degrades the potentially harmful beta-amyloid peptide. Work with ADAM10-deficient mice supports a role in Notch signalling.


entry: 3.4.24.82
name: --- - ADAMTS-4 endopeptidase - aggrecanase-1
comment:
In peptidase family M12. Thought to be biologically significant for the degradation of the aggrecan component of cartilage matrix.

reaction:
Glutamyl endopeptidase; bonds cleaved include -Thr-Glu-Gly-Glu373-|-Ala-Arg-Gly-Ser- in the interglobular domain of mammalian aggrecan


entry: 3.4.24.83
name: --- - anthrax lethal factor endopeptidase - lethal toxin
comment:
From the bacterium Bacilus anthracis that causes anthrax. One of three proteins that are collectively termed anthrax toxin. Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. In peptidase family M34.

reaction:
Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases


entry: 3.4.24.84
name: --- - Ste24 endopeptidase
comment:
Type example of peptidase family M48. One of two enzymes that can catalyse this processing step for mating a-factor in yeast. Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor.

reaction:
The peptide bond hydrolysed can be designated -C-|-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids


entry: 3.4.24.85
name: --- - S2P endopeptidase
comment:
Type example of peptidase family M50. The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus. This enzyme cleaves the second of these, and is thus the "site 2 protease", S2P.

reaction:
Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site DRSRILL483-|-CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.


entry: 3.4.24.86
name: --- - ADAM 17 endopeptidase - tumor necrosis factor alpha-converting enzyme - TACE
comment:
In peptidase family M12. In vivo, the cleavage of tumor necrosis factor alpha precursor releases the soluble, 17-kDa TNFalpha, which induces inflammation.

reaction:
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNFalpha). Similarly cleaves other membrane-anchored, cell-surface proteins to "shed" the extracellular domains


entry: 3.4.25.1
reaction: Cleavage of peptide bonds with very broad specificity
name:
--- 
- proteasome endopeptidase complex
- ingensin
- macropain
- multicatalytic endopeptidase complex
- prosome
- multicatalytic proteinase (complex)
- MCP
- proteasome
- large multicatalytic protease
- multicatalytic proteinase
- proteasome organelle
- alkaline protease
- 26S protease
- tricorn proteinase
- tricorn protease

comment:
A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the specificity of proteolysis, perhaps optimizing it for the formation of antigenic peptides. A complex of the 20-S proteasome endopeptidase complex with a 19-S regulatory unit is the 26-S proteasome that degrades ubiquitin-protein conjugates. Type example of peptidase family T1. Formerly EC 3.4.24.5, EC 3.4.22.21 and EC 3.4.99.46


entry: 3.4.99.1
name: --- - Transferred to 3.4.23.28
comment:
Transferred entry: now EC 3.4.23.28 - acrocylindropepsin (EC 3.4.99.1 created 1972, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.99.10
name: --- - Transferred to 3.4.24.56
comment:
Transferred entry: now EC 3.4.24.56 - insulysin (EC 3.4.99.10 created 1972, transferred 1976 to EC 3.4.22.11, transferred 1978 to EC 3.4.99.45, transferred 1993 to EC 3.4.24.56)


entry: 3.4.99.11
name: --- - Deleted entry
comment:
Deleted entry: streptomyces alkalophilic keratinase (EC 3.4.99.11 created 1965 as EC 3.4.4.25, transferred 1972 to EC 3.4.99.11, deleted 1992)


entry: 3.4.99.12
name: --- - Deleted entry
comment:
Deleted entry: trichophyton mentagrophytes keratinase (EC 3.4.99.12 created 1972, deleted 1978 [transferred to EC 3.4.24.10, deleted 1992])


entry: 3.4.99.13
name: --- - Transferred to 3.4.24.32
comment:
Transferred entry: now EC 3.4.24.32 - beta-lytic metalloendopeptidase (EC 3.4.99.13 created 1972, deleted 1978 [transferred to EC 3.4.24.4, deleted 1992])


entry: 3.4.99.15
name: --- - Deleted entry
comment:
Deleted entry: paecilomyces proteinase (EC 3.4.99.15 created 1972, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.99.16
name: --- - Deleted entry
comment:
Deleted entry: penicillium notatum extracellular proteinase (EC 3.4.99.16 created 1972, deleted 1992)


entry: 3.4.99.22
name: --- - Transferred to 3.4.24.29
comment:
Transferred entry: now EC 3.4.24.29 - aureolysin (EC 3.4.99.22 created 1972, modified 1976, deleted 1978 [transferred to EC 3.4.24.4, deleted 1992])


entry: 3.4.99.24
name: --- - Deleted entry
comment:
Deleted entry: Tenebrio alpha-proteinase (EC 3.4.99.24 created 1972, deleted 1978 [transferred to EC 3.4.21.18, deleted 1992])


entry: 3.4.99.25
name: --- - Transferred to 3.4.23.21
comment:
Transferred entry: now included with EC 3.4.23.21 - rhizopuspepsin (EC 3.4.99.25 created 1972, deleted 1978 [transferred to EC 3.4.23.6, deleted 1992])


entry: 3.4.99.26
name: --- - Transferred to 3.4.21.73 and 3.4.21.68
comment:
Transferred entry: now EC 3.4.21.73 - u-plasminogen activator and EC 3.4.21.68 - t-plasminogen activator (EC 3.4.99.26 created 1972, deleted 1978 [transferred to EC 3.4.21.31, deleted 1992])


entry: 3.4.99.27
name: --- - Deleted entry
comment:
Deleted entry: Echis carinatus prothrombin-activating proteinase (EC 3.4.99.27 created 1978, deleted 1992)


entry: 3.4.99.30
name: --- - Transferred to 3.4.24.20
comment:
Transferred entry: now included in EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase (EC 3.4.99.30 created 1978, deleted 1992)


entry: 3.4.99.31
name: --- - Transferred to 3.4.24.15
comment:
Transferred entry: now included with EC 3.4.24.15 - thimet oligopeptidase (EC 3.4.99.31 created 1978, deleted 1992)


entry: 3.4.99.32
name: --- - Transferred to 3.4.24.20
comment:
Transferred entry: now EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase (EC 3.4.99.32 created 1978, deleted 1992)


entry: 3.4.99.33
name: --- - Deleted entry
comment:
Deleted entry: cathepsin R (EC 3.4.99.33 created 1981, deleted 1984 [transferred to EC 3.4.21.52, deleted 1992])


entry: 3.4.99.38
name: --- - Transferred to 3.4.23.17
comment:
Transferred entry: now EC 3.4.23.17 - pro-opiomelanocortin converting enzyme (EC 3.4.99.38 created 1989, deleted 1992)


entry: 3.4.99.41
name: --- - Transferred to 3.4.24.64
comment:
Transferred entry: now EC 3.4.24.64 - mitochondrial processing peptidase (EC 3.4.99.41 created 1989/90, deleted 1995)


entry: 3.4.99.46
name: --- - Transferred to 3.4.25.1
comment:
Transferred entry: now EC 3.4.25.1- proteasome endopeptidase complex (EC 3.4.99.46 created 1992, deleted 2000)


entry: 3.4.-.-
name: --- []
reaction:
(1) N6,N6,N6-Trimethyl-L-lysine + Protein <=> Protein N6,N6,N6-trimethyl-L-lysine + H2O [RN:R04313]; (2) N6-D-Biotinyl-L-lysine + Peptide <=> Holo-[carboxylase] [RN:R04869]


entry: 3.5.1.1
sysname: L-asparagine amidohydrolase
reaction: L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
iubmb_reaction: R00485
kegg_reaction: R06134
name:
--- 
- asparaginase
- asparaginase II
- L-asparaginase
- colaspase
- elspar
- leunase
- crasnitin
- alpha-asparaginase


entry: 3.5.1.4
sysname: acylamide amidohydrolase
reaction: A monocarboxylic acid amide + H2O = a monocarboxylate + NH3 [RN:R03909]
iubmb_reaction: R03909 > R00321 R02540 R03096 R03180 R05551 R05590
kegg_reaction: R06134
name:
--- 
- amidase
- acylamidase
- acylase
- amidohydrolase
- deaminase
- fatty acylamidase
- N-acetylaminohydrolase


entry: 3.5.1.9
sysname: aryl-formylamine amidohydrolase
comment: Also acts on other aromatic formylamines.
reaction: N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959]
iubmb_reaction: R01959
kegg_reaction: R00988 R04911
name:
--- 
- arylformamidase
- kynurenine formamidase
- formylase
- formylkynureninase
- formylkynurenine formamidase
- formamidase I
- formamidase II


entry: 3.5.1.11
sysname: penicillin amidohydrolase
reaction: penicillin + H2O = a carboxylate + 6-aminopenicillanate [RN:R02170]
iubmb_reaction: R02170
kegg_reaction: R04103
name:
--- 
- penicillin amidase
- penicillin acylase
- benzylpenicillin acylase
- novozym 217
- semacylase
- alpha-acylamino-beta-lactam acylhydrolase
- ampicillin acylase


entry: 3.5.1.13
sysname: aryl-acylamide amidohydrolase
comment: Also acts on 4-substituted anilides.
reaction: An anilide + H2O = a carboxylate + aniline [RN:R01862]
iubmb_reaction: R01862
name:
--- 
- aryl-acylamidase
- AAA-1
- AAA-2
- brain acetylcholinesterase (is associated with AAA-2)
- pseudocholinesterase (associated with arylacylamidase)


entry: 3.5.1.14
sysname: N-acyl-L-amino-acid amidohydrolase
comment: Wide specificity; also hydrolyses dehydropeptides. Used in separating D- and L- amino acids
reaction: An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid [RN:R01263]
iubmb_reaction: R01263 > R00669
name:
--- 
- aminoacylase
- dehydropeptidase II
- histozyme
- hippuricase
- benzamidase
- acylase I
- hippurase
- amido acid deacylase
- L-aminoacylase
- acylase
- aminoacylase I
- L-amino-acid acylase
- alpha-N-acylaminoacid hydrolase
- long acyl amidoacylase
- short acyl amidoacylase


entry: 3.5.1.15
sysname: N-acyl-L-aspartate amidohydrolase
reaction: N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate [RN:R00546]
iubmb_reaction: R00546 > R00488 R00526
name:
--- 
- aspartoacylase
- aminoacylase II
- N-acetylaspartate amidohydrolase
- acetyl-aspartic deaminase
- acylase II


entry: 3.5.1.18
sysname: N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
reaction: N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate [RN:R02734]
iubmb_reaction: R02734
name:
--- 
- succinyl-diaminopimelate desuccinylase
- N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase


entry: 3.5.1.20
sysname: L-citrulline 5-N-carbamoyldihydrolase
reaction: L-citrulline + H2O = L-ornithine + CO2 + NH3 [RN:R00665]
iubmb_reaction: R00665
kegg_reaction: R06134
name:
--- 
- citrullinase
- citrulline ureidase
- citrulline hydrolase
- L-citrulline N5-carbamoyldihydrolase


entry: 3.5.1.24
name: --- - choloylglycine hydrolase - glycocholase - bile salt hydrolase - choloyltaurine hydrolase
sysname: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine amidohydrolase
comment: Also acts on the 3alpha,12alpha-dihydroxy-derivative, and on choloyl-taurine.
iubmb_reaction: R05835
kegg_reaction: R02797 R03975 R03977 R04486 R04487
reaction:
3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine + H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine [RN:R05835]


entry: 3.5.1.25
sysname: N-acetyl-D-glucosamine-6-phosphate amidohydrolase
reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate [RN:R02059]
iubmb_reaction: R02059
kegg_reaction: R05168
name:
--- 
- N-acetylglucosamine-6-phosphate deacetylase
- acetylglucosamine phosphate deacetylase
- acetylaminodeoxyglucosephosphate acetylhydrolase
- 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase


entry: 3.5.1.26
sysname: N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
iubmb_reaction: R03421
name:
--- 
- N4-(beta-N-acetylglucosaminyl)-L-asparaginase
- aspartylglucosylamine deaspartylase
- aspartylglucosylaminase
- aspartylglucosaminidase
- aspartylglycosylamine amidohydrolase
- N-aspartyl-beta -glucosaminidase
- glucosylamidase
- beta -aspartylglucosylamine amidohydrolase

comment:
Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free alpha-amino and alpha-carboxyl groups [cf. EC 3.5.1.52 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase]

reaction:
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate [RN:R03421]


entry: 3.5.1.28
sysname: peptidoglycan amidohydrolase
iubmb_reaction: (other) R04112
kegg_reaction: R04112
name:
--- 
- N-acetylmuramoyl-L-alanine amidase
- acetylmuramyl-L-alanine amidase
- N-acetylmuramyl-L-alanine amidase
- N-acylmuramyl-L-alanine amidase
- acetylmuramoyl-alanine amidase
- N-acetylmuramic acid L-alanine amidase
- acetylmuramyl-alanine amidase
- N-acetylmuramylalanine amidase
- murein hydrolase
- N-acetylmuramoyl-L-alanine amidase type I
- N-acetylmuramoyl-L-alanine amidase type II

reaction:
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides


entry: 3.5.1.29
sysname: 2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
comment: Involved in the degradation of pyridoxin in Pseudomonas.
reaction: 2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2 [RN:R01649]
iubmb_reaction: R01649
kegg_reaction: R06134
name:
--- 
- 2-(acetamidomethylene)succinate hydrolase
- alpha-(N-acetylaminomethylene)succinic acid hydrolase


entry: 3.5.1.30
name: --- - 5-aminopentanamidase - 5-aminovaleramidase - 5-aminonorvaleramidase
sysname: 5-aminopentanamide amidohydrolase
reaction: 5-aminopentanamide + H2O = 5-aminopentanoate + NH3 [RN:R02273]
iubmb_reaction: R02273
kegg_reaction: R06134
comment:
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.


entry: 3.5.1.33
sysname: N-acetyl-D-glucosamine amidohydrolase
reaction: N-acetyl-D-glucosamine + H2O = D-glucosamine + acetate [RN:R01200]
iubmb_reaction: R01200
name:
--- 
- N-acetylglucosamine deacetylase
- acetylaminodeoxyglucose acetylhydrolase
- N-acetyl-D-glucosaminyl N-deacetylase


entry: 3.5.1.34
name: --- - Deleted entry
comment:
Deleted entry: acetylhistidine deacetylase. Identical with EC 3.4.13.5 X-methyl-His dipeptidase (EC 3.5.1.34 created 1972, deleted 1981)


entry: 3.5.1.37
name: --- - Deleted entry
comment:
Deleted entry: 4-L-aspartylglycosylamine amidohydrolase. Identical with EC 3.5.1.26 N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.37 created 1972, deleted 1976)


entry: 3.5.1.38
name: --- - glutamin-(asparagin-)ase
sysname: L-glutamine(L-asparagine) amidohydrolase
reaction: L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
iubmb_reaction: R00256
kegg_reaction: R00485 R00490 R01579 R06134
comment:
L-Asparagine is hydrolysed at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly.


entry: 3.5.1.39
name: --- - alkylamidase
sysname: N-methylhexanamide amidohydrolase
reaction: N-methylhexanamide + H2O = hexanoate + methylamine [RN:R03620]
iubmb_reaction: R03620
comment:
The enzyme hydrolyses N-monosubstituted and N,N-disubstituted amides, and there is some activity towards primary amides. It has little or no activity towards short-chain substrates.


entry: 3.5.1.42
sysname: nicotinamide-D-ribonucleotide amidohydrolase
comment: Also acts more slowly on beta-nicotinamide D-ribonucleoside.
reaction: beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate D-ribonucleotide + NH3 [RN:R02322]
iubmb_reaction: R02322
kegg_reaction: R06134
name:
--- 
- nicotinamide-nucleotide amidase
- NMN deamidase
- nicotinamide mononucleotide deamidase
- nicotinamide mononucleotide amidohydrolase


entry: 3.5.1.43
name: --- - peptidyl-glutaminase - peptidoglutaminase I - peptideglutaminase - peptidoglutaminase
sysname: peptidyl-L-glutamine amidohydrolase
reaction: alpha-N-peptidyl-L-glutamine + H2O = alpha-N-peptidyl-L-glutamate + NH3 [RN:R04341]
iubmb_reaction: R04341
kegg_reaction: R06134
comment:
Specific for the hydrolysis of the gamma-amide of glutamine substituted at the alpha-amino group, e.g., glycyl-L-glutamine, N-acetyl-L-glutamine and L-leucylglycyl-L-glutamine.


entry: 3.5.1.44
sysname: protein-L-glutamine amidohydrolase
reaction: protein L-glutamine + H2O = protein L-glutamate + NH3 [RN:R02622]
iubmb_reaction: R02622
kegg_reaction: R06134
name:
--- 
- protein-glutamine glutaminase
- peptidoglutaminase II
- glutaminyl-peptide glutaminase
- destabilase
- peptidylglutaminase II

comment:
Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L-glutaminylglycine.


entry: 3.5.1.45
name: --- - Deleted entry
comment:
Deleted entry: urease (ATP-hydrolysing). Now listed only as EC 6.3.4.6 urea carboxylase (EC 3.5.1.45 created 1978, deleted 1986)


entry: 3.5.1.46
name: --- - 6-aminohexanoate-dimer hydrolase - 6-aminohexanoic acid oligomer hydrolase
sysname: N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
reaction: N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate [RN:R00059]
iubmb_reaction: R00059
comment:
Also hydrolyses oligomers of 6-aminohexanoate containing up to six residues, but more slowly; the residues are removed sequentially from the N-terminus.


entry: 3.5.1.47
sysname: N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase
reaction: N-acetyl-LL-2,6-diaminoheptanedioate + H2O = acetate + LL-2,6-diaminoheptanedioate [RN:R02733]
iubmb_reaction: R02733
name:
--- 
- N-acetyldiaminopimelate deacetylase
- N-acetyl-L-diaminopimelic acid deacylase
- N-acetyl-LL-diaminopimelate deacylase


entry: 3.5.1.48
sysname: N8-acetylspermidine amidohydrolase
reaction: N8-acetylspermidine + H2O = acetate + spermidine [RN:R07300]
iubmb_reaction: R07300
kegg_reaction: R01916
name:
--- 
- acetylspermidine deacetylase
- N8-monoacetylspermidine deacetylase
- N8-acetylspermidine deacetylase
- N-acetylspermidine deacetylase
- N1-acetylspermidine amidohydrolase (incorrect)

comment:
It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction [1] but this has since been disproved by Marchant et al. [3].


entry: 3.5.1.50
name: --- - pentanamidase - valeramidase
sysname: pentanamide amidohydrolase
reaction: pentanamide + H2O = pentanoate + NH3 [RN:R02938]
iubmb_reaction: R02938
comment:
Also acts, more slowly, on other short-chain aliphatic amides. Different from EC 3.5.1.49 formamidase.


entry: 3.5.1.51
sysname: 4-acetamidobutanoyl-CoA amidohydrolase
comment: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA [RN:R04056]
iubmb_reaction: R04056
name:
--- 
- 4-acetamidobutyryl-CoA deacetylase
- aminobutyryl-CoA thiolesterase
- deacetylase-thiolesterase


entry: 3.5.1.52
sysname: N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase
name:
--- 
- peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
- glycopeptide N-glycosidase
- glycopeptidase
- N-oligosaccharide glycopeptidase
- N-glycanase
- Jack-bean glycopeptidase
- PNGase A
- PNGase F

comment:
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26 N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.

reaction:
Hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue


entry: 3.5.1.54
name: --- - allophanate hydrolase - allophanate lyase
sysname: urea-1-carboxylate amidohydrolase
reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3 [RN:R00005]
iubmb_reaction: R00005
comment:
The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6 urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate.


entry: 3.5.1.55
sysname: N-long-chain-fatty-acyl-L-glutamate amidohydrolase
reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate [RN:R02040]
iubmb_reaction: R02040
name:
--- 
- long-chain-fatty-acyl-glutamate deacylase
- long-chain aminoacylase
- long-chain acylglutamate amidase
- N-acyl-D-glutamate deacylase

comment:
Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.


entry: 3.5.1.56
name: --- - N,N-dimethylformamidase - dimethylformamidase - DMFase
sysname: N,N-dimethylformamide amidohydrolase
reaction: N,N-dimethylformamide + H2O = dimethylamine + formate [RN:R02509]
iubmb_reaction: R02509
comment:
An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.


entry: 3.5.1.58
sysname: N-benzyloxycarbonylglycine urethanehydrolase
reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine [RN:R02551]
iubmb_reaction: R02551
name:
--- 
- N-benzyloxycarbonylglycine hydrolase
- benzyloxycarbonylglycine hydrolase
- N(alpha)-carbobenzoxyamino acid amidohydrolase
- N(alpha)-benzyloxycarbonyl amino acid urethane hydrolase
- N(alpha)-benzyloxycarbonyl amino acid urethane hydrolase I

comment:
Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64 N(alpha)-benzyloxycarbonylleucine hydrolase.


entry: 3.5.1.60
sysname: N-(long-chain-acyl)ethanolamine amidohydrolase
comment: Does not act on N-acylsphingosine or N,O-diacylethanolamine.
reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine [RN:R02041]
iubmb_reaction: R02041
name:
--- 
- N-(long-chain-acyl)ethanolamine deacylase
- N-acylethanolamine amidohydrolase
- acylethanolamine amidase


entry: 3.5.1.61
name: --- - mimosinase
sysname: mimosine amidohydrolase
comment: An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
iubmb_reaction: R04350
reaction:
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O = 3-hydroxy-4H-pyrid-4-one + L-serine [RN:R04350]


entry: 3.5.1.62
name: --- - acetylputrescine deacetylase
sysname: N-acetylputrescine acetylhydrolase
reaction: N-acetylputrescine + H2O = acetate + putrescine [RN:R01156]
iubmb_reaction: R01156
comment:
The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.


entry: 3.5.1.64
sysname: N(alpha)-benzyloxycarbonyl-L-leucine urethanehydrolase
reaction: N(alpha)-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine [RN:R02552]
iubmb_reaction: R02552
name:
--- 
- N(alpha)-benzyloxycarbonylleucine hydrolase
- benzyloxycarbonylleucine hydrolase
- N(alpha)-benzyloxycarbonyl amino acid urethane hydrolase IV

comment:
Also acts on N(alpha)-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.


entry: 3.5.1.66
sysname: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
comment: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
iubmb_reaction: R04397
name:
--- 
- 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
- compound B hydrolase
- alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid hydrolase

reaction:
2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2 [RN:R04397]


entry: 3.5.1.67
sysname: 4-methylene-L-glutamine amidohydrolase
reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3 [RN:R02712]
iubmb_reaction: R02712
name:
--- 
- 4-methyleneglutaminase
- 4-methyleneglutamine deamidase
- 4-methyleneglutamine amidohydrolase


entry: 3.5.1.68
sysname: N-formyl-L-glutamate amidohydrolase
comment: The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine.
reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate [RN:R00525]
iubmb_reaction: R00525
name:
--- 
- N-formylglutamate deformylase
- beta-citryl-L-glutamate hydrolase
- formylglutamate deformylase
- N-formylglutamate hydrolase
- beta-citrylglutamate amidase
- beta-citryl-L-glutamate amidohydrolase
- beta-citryl-L-glutamate amidase
- beta-citryl-L-glutamate-hydrolyzing enzyme


entry: 3.5.1.69
name: --- - glycosphingolipid deacylase - glycosphingolipid ceramide deacylase
sysname: glycosphingolipid amidohydrolase
comment: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
reaction:
Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives


entry: 3.5.1.70
name: --- - aculeacin-A deacylase - aculeacin A acylase
sysname: aculeacin-A amidohydrolase
reaction:
Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain


entry: 3.5.1.71
name: --- - N-feruloylglycine deacylase - N-feruloylglycine hydrolase
sysname: N-feruloylglycine amidohydrolase
reaction: N-feruloylglycine + H2O = ferulate + glycine [RN:R03579]
iubmb_reaction: R03579
comment:
Hydrolyses a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14 aminoacylase.


entry: 3.5.1.76
name: --- - arylalkyl acylamidase - aralkyl acylamidase
sysname: N-acetylarylalkylamine amidohydrolase
reaction: N-acetylarylalkylamine + H2O = arylalkylamine + acetate [RN:R04727]
iubmb_reaction: R04727
comment:
identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase.


entry: 3.5.1.77
name: --- - N-carbamoyl-D-amino acid hydrolase
sysname: N-carbamoyl-D-amino acid amidohydrolase
reaction: N-carbamoyl-D-amino acid + H2O = D-amino acid + NH3 + CO2 [RN:R02190]
iubmb_reaction: R02190
comment:
has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropionate, which are substrates for other amidohydrolases.


entry: 3.5.1.78
name: --- - glutathionylspermidine amidase - glutathionylspermidine amidohydrolase (spermidine-forming)
sysname: gamma-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
reaction: glutathionylspermidine + H2O = glutathione + spermidine [RN:R01918]
iubmb_reaction: R01918
comment:
spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.


entry: 3.5.1.79
name: --- - phthalyl amidase
sysname: phthalyl-amide amidohydrolase
reaction: a phthalylamide + H2O = phthalic acid + a substituted amine [RN:R05167]
iubmb_reaction: R05167
comment:
in the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required


entry: 3.5.1.80
name: --- - Deleted entry
comment:
Deleted entry: identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created 1999, deleted 2002)


entry: 3.5.1.81
name: --- - N-acyl-D-amino-acid deacylase
sysname: N-acyl-D-amino acid amidohydrolase
reaction: N-acyl-D-amino acid + H2O = an acid + D-amino acid [RN:R02192]
iubmb_reaction: R02192
comment:
the enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.


entry: 3.5.1.82
name: --- - N-acyl-D-glutamate deacylase
sysname: N-acyl-D-glutamate amidohydrolase
reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate [RN:R01581]
iubmb_reaction: R01581
comment:
the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.


entry: 3.5.1.83
name: --- - N-acyl-D-aspartate deacylase
sysname: N-acyl-D-aspartate amidohydrolase
reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate [RN:R02182]
iubmb_reaction: R02182
comment:
the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.


entry: 3.5.1.84
name: --- - biuret amidohydrolase
sysname: biuret amidohydrolase
reaction: biuret + H2O = urea + CO2 + NH3 [RN:R05562]
iubmb_reaction: R05562
kegg_reaction: R05563
comment:
Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria.


entry: 3.5.1.85
name: --- - (S)-N-acetyl-1-phenylethylamine hydrolase - (S)-N-acetyl-1-phenylethylamine amidohydrolase
sysname: (S)-N-acetylphenylethylamine:H2O hydrolase
reaction: N-acetylphenylethylamine + H2O = phenylethylamine + acetate [RN:R07301]
iubmb_reaction: R07301
comment:
Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.


entry: 3.5.1.87
name: --- - N-carbamoyl-L-amino-acid hydrolase
sysname: N-carbamoyl-L-amino acid amidohydrolase
reaction: N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = L-2-amino acid + NH3 + CO2 [RN:R05782]
iubmb_reaction: R05782
comment:
The enzyme has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. Carbamoyl-L-valine is the best substrate. It is inactive on derivatives of D-amino acids, the substrates of EC 3.5.1.77 (N-carbamoyl-D-amino acid hydrolase), or on N-carbamoyl-beta-alanine, the substrate of EC 3.5.1.6 (beta-ureidopropionase). The enzyme hydrolyses formyl derivatives rapidly, and acetyl derivatives very slowly. Mn2+, Ni2+ or Co2+ enabled reactivation of enzyme that had been treated with a chelating agent.


entry: 3.5.1.88
name: --- - peptide deformylase
sysname: formyl-L-methionyl peptide amidohydrolase
reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide [RN:R05635]
iubmb_reaction: R05635
comment:
Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.27 (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31 (formylmethionine deformylase).


entry: 3.5.1.89
sysname: 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase
iubmb_reaction: R03482 R05917(G)
name:
--- 
- N-acetylglucosaminylphosphatidylinositol deacetylase
- N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase
- N-acetylglucosaminylphosphatidylinositol de-N-acetylase
- GlcNAc-PI de-N-acetylase
- GlcNAc-PI deacetylase
- acetylglucosaminylphosphatidylinositol deacetylase

comment:
Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.

reaction:
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate [RN:R03482 R05917]


entry: 3.5.1.90
name: --- - adenosylcobinamide hydrolase - CbiZ - AdoCbi amidohydrolase
sysname: adenosylcobinamide amidohydrolase
reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol [RN:R05226]
iubmb_reaction: R05226
comment:
Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).


entry: 3.5.1.91
name: --- - N-substituted formamide deformylase - NfdA
sysname: N-benzylformamide amidohydrolase
reaction: N-benzylformamide + H2O = formate + benzylamine [RN:R07303]
iubmb_reaction: R07303
comment:
Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.


entry: 3.5.1.92
name: --- - pantetheine hydrolase - pantetheinase - vanin - vanin-1
sysname: (R)-pantetheine amidohydrolase
reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol [RN:R02973]
iubmb_reaction: R02973
comment:
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol, a potent anti-oxidant [5].


entry: 3.5.1.93
sysname: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
iubmb_reaction: R07402
name:
--- 
- glutaryl-7-aminocephalosporanic-acid acylase
- 7beta-(4-carboxybutanamido)cephalosporanic acid acylase
- cephalosporin C acylase
- glutaryl-7-ACA acylase
- CA
- GCA
- GA
- cephalosporin acylase
- glutaryl-7-aminocephalosporanic acid acylase
- GL-7-ACA acylase

comment:
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.

reaction:
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate [RN:R07402]


entry: 3.5.1.94
name: --- - gamma-glutamyl-gamma-aminobutyrate hydrolase - gamma-glutamyl-GABA hydrolase - PuuD - YcjL
sysname: 4-(glutamylamino)butanoate amidohydrolase
reaction: 4-(glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate
iubmb_reaction: (other) R07419
kegg_reaction: R07419
comment:
Forms part of a novel putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form gamma-glutamylputrescine, which is oxidized to 4-(glutamylamino)butanal and then to 4-(glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase).


entry: 3.5.1.95
name: --- - N-malonylurea hydrolase - ureidomalonase
sysname: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea
comment:
Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).


entry: 3.5.1.96
name: --- - succinylglutamate desuccinylase - N2-succinylglutamate desuccinylase - SGDS - AstE
sysname: N-succinyl-L-glutamate amidohydrolase
reaction: N-succinyl-L-glutamate + H2O = succinate + L-glutamate [RN:R00411]
iubmb_reaction: R00411
comment:
Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).


entry: 3.5.1.-
name: --- []
reaction:
(1) Maleic acid + NH3 <=> Maleamate + H2O [RN:R03540]; (2) UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine + H2O <=> UDP-3-O-(3-hydroxytetradecanoyl)-D-glucosamine + Acetate [RN:R04587]; (3) N-(5'-Phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-D- ribosyl)-4-imidazolecarboxamide + H2O <=> 5'-Phospho-D-1-ribulosylformimine + 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [RN:R04655]; (4) N2-Acetyl-L-lysine + H2O <=> L-Lysine + Acetate [RN:R06845]; (5) N-Cyclohexylformamide + H2O <=> Cyclohexylamine + Formate [RN:R06940]


entry: 3.5.2.1
name: --- - barbiturase
sysname: barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
reaction: barbiturate + H2O = 3-oxo-3-ureidopropanoate [RN:R02139]
iubmb_reaction: R02139
kegg_reaction: R03870
comment:
Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.


entry: 3.5.2.2
sysname: 5,6-dihydropyrimidine amidohydrolase
comment: Also acts on dihydrothymine and hydantoin.
reaction: 5,6-dihydrouracil + H2O = N-carbamoyl-beta-alanine [RN:R02269]
iubmb_reaction: R02269
kegg_reaction: R03055
name:
--- 
- dihydropyrimidinase
- hydantoinase
- hydropyrimidine hydrase
- hydantoin peptidase
- pyrimidine hydrase
- D-hydantoinase


entry: 3.5.2.6
sysname: beta-lactam hydrolase
reaction: A beta-lactam + H2O = a substituted beta-amino acid [RN:R03743]
iubmb_reaction: R03743 > R06363
name:
--- 
- beta-lactamase
- penicillinase
- cephalosporinase
- neutrapen
- penicillin beta-lactamase
- exopenicillinase
- ampicillinase
- penicillin amido-beta-lactamhydrolase
- penicillinase I, II
- beta-lactamase I-III
- beta-lactamase A, B, C
- beta-lactamase AME I
- cephalosporin-beta-lactamase

comment:
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.


entry: 3.5.2.7
sysname: 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase
iubmb_reaction: R02288
name:
--- 
- imidazolonepropionase
- 4(5)-imidazolone-5(4)-propionic acid hydrolase
- imidazolone propionic acid hydrolase

reaction:
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+ [RN:R02288]


entry: 3.5.2.8
name: --- - Deleted entry
comment:
Deleted entry: cephalosporinase. Now included with EC 3.5.2.6 beta-lactamase (EC 3.5.2.8 created 1972, deleted 1978)


entry: 3.5.2.9
sysname: 5-oxo-L-proline amidohydrolase (ATP-hydrolysing)
reaction: ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate [RN:R07304]
iubmb_reaction: R07304
kegg_reaction: R00251
name:
--- 
- 5-oxoprolinase (ATP-hydrolysing)
- pyroglutamase (ATP-hydrolysing)
- oxoprolinase
- pyroglutamase
- 5-oxoprolinase
- pyroglutamate hydrolase
- pyroglutamic hydrolase
- L-pyroglutamate hydrolase
- 5-oxo-L-prolinase


entry: 3.5.2.13
name: --- - 2,5-dioxopiperazine hydrolase - cyclo(Gly-Gly) hydrolase - cyclo(glycylglycine) hydrolase
sysname: 2,5-dioxopiperazine amidohydrolase
reaction: 2,5-dioxopiperazine + H2O = glycylglycine [RN:R03810]
iubmb_reaction: R03810
comment:
Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates.


entry: 3.5.2.14
sysname: N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing)
reaction: ATP + N-methylimidazolidine-2,4-dione + 2 H2O = ADP + phosphate + N-carbamoylsarcosine [RN:R03187]
iubmb_reaction: R03187
name:
--- 
- N-methylhydantoinase (ATP-hydrolysing)
- N-methylhydantoin amidohydrolase
- methylhydantoin amidase
- N-methylhydantoin hydrolase
- N-methylhydantoinase


entry: 3.5.2.16
sysname: cyclic-imide amidohydrolase (decyclizing)
reaction: maleimide + H2O = maleamic acid [RN:R05781]
iubmb_reaction: R05781
name:
--- 
- maleimide hydrolase
- imidase
- cyclic imide hydrolase
- cyclic-imide amidohydrolase (decyclicizing) [misprint]

comment:
Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase.


entry: 3.5.2.17
name: --- - hydroxyisourate hydrolase - HIUHase - 5-hydroxyisourate hydrolase
sysname: 5-hydroxyisourate amidohydrolase
iubmb_reaction: R06601
comment:
The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.

reaction:
5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate [RN:R06601]


entry: 3.5.2.-
name: --- []
reaction:
(1) Xanthine + H2O <=> 5-Ureido-4-imidazole carboxylate [RN:R02141]; (2) N-Formiminoglycine <=> Imidazolone + H2O [RN:R04026]; (3) N-Formimino-L-aspartate <=> 4-Imidazolone-5-acetate + H2O [RN:R04214]; (4) epsilon-Caprolactam + H2O <=> 6-Aminohexanoate [RN:R05356]


entry: 3.5.3.7
sysname: 4-guanidinobutanoate amidinohydrolase
comment: Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidinohexanoate.
reaction: 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea [RN:R01990]
iubmb_reaction: R01990
name:
--- 
- guanidinobutyrase
- gamma-guanidobutyrase
- 4-guanidinobutyrate amidinobutyrase
- gamma-guanidinobutyrate amidinohydrolase
- G-Base
- GBH
- guanidinobutyrate ureahydrolase


entry: 3.5.3.8
sysname: N-formimidoyl-L-glutamate formimidoylhydrolase
reaction: N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide [RN:R02285]
iubmb_reaction: R02285
name:
--- 
- formimidoylglutamase
- formiminoglutamase
- N-formiminoglutamate hydrolase
- N-formimino-L-glutamate formiminohydrolase


entry: 3.5.3.12
name: --- - agmatine deiminase - agmatine amidinohydrolase
sysname: agmatine iminohydrolase
reaction: agmatine + H2O = N-carbamoylputrescine + NH3 [RN:R01416]
iubmb_reaction: R01416
kegg_reaction: R06138
comment:
The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.


entry: 3.5.3.13
sysname: N-formimidoyl-L-glutamate iminohydrolase
reaction: N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3 [RN:R02286]
iubmb_reaction: R02286
kegg_reaction: R06138
name:
--- 
- formimidoylglutamate deiminase
- formiminoglutamate deiminase
- formiminoglutamic iminohydrolase


entry: 3.5.3.18
sysname: N(G),N(G)-dimethyl-L-arginine dimethylamidohydrolase
comment: Also acts on N(G)-monomethyl-L-arginine.
reaction: N(G),N(G)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline [RN:R02513]
iubmb_reaction: R02513
name:
--- 
- dimethylargininase
- dimethylarginine dimethylaminohydrolase
- N(G),N(G)-dimethylarginine dimethylaminohydrolase


entry: 3.5.3.21
name: --- - methylenediurea deaminase - methylenediurease
sysname: methylenediurea aminohydrolase
iubmb_reaction: R05170 R05171 R05172
kegg_reaction: R05169
comment:
The methylenediurea is hydrolysed and decarboxylated to give an aminated methylurea, which then spontaneously hydrolyses to hydroxymethylurea. The enzyme from Ochrobactrum anthropi also hydrolyses dimethylenetriurea and trimethylenetetraurea as well as ureidoglycolate, which is hydrolysed to urea and glyoxylate, and allantoate, which is hydrolysed to ureidoglycolate, ammonia and carbon dioxide.

reaction:
(1) NH2-CO-NH-CH2-NH-CO-NH2 + H2O = N-(carboxyaminomethyl)urea + NH3 [RN:R05170]; (2) N-(carboxyaminomethyl)urea = N-(aminomethyl)urea + CO2 (spontaneous) [RN:R05171]; (3) N-(aminomethyl)urea + H2O = N-(hydroxymethyl)urea + NH3 (spontaneous) [RN:R05172]


entry: 3.5.3.22
name: --- - proclavaminate amidinohydrolase - PAH - proclavaminate amidino hydrolase
sysname: amidinoproclavaminate amidinohydrolase
reaction: amidinoproclavaminate + H2O = proclavaminate + urea [RN:R05357]
iubmb_reaction: R05357
comment:
Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme. Requires Mn2+.


entry: 3.5.3.23
sysname: N2-succinyl-L-arginine iminohydrolase (decarboxylating)
reaction: N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2 [RN:R04189]
iubmb_reaction: R04189
name:
--- 
- N-succinylarginine dihydrolase
- N2-succinylarginine dihydrolase
- arginine succinylhydrolase
- SADH
- AruB
- AstB

comment:
Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).


entry: 3.5.4.6
sysname: AMP aminohydrolase
comment: cf. EC 3.5.4.17 adenosine-phosphate deaminase.
reaction: AMP + H2O = IMP + NH3 [RN:R00181]
iubmb_reaction: R00181
kegg_reaction: R06137
name:
--- 
- AMP deaminase
- adenylic acid deaminase
- AMP aminase
- adenylic deaminase
- adenylate deaminase
- 5-AMP deaminase
- adenosine 5-monophosphate deaminase
- 5-adenylate deaminase
- adenyl deaminase
- 5-adenylic acid deaminase
- adenosine monophosphate deaminase
- adenylate aminohydrolase
- adenylate desaminase
- adenosine 5-phosphate aminohydrolase


entry: 3.5.4.9
sysname: 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing)
reaction: 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate [RN:R01655]
iubmb_reaction: R01655
kegg_reaction: R00943
name:
--- 
- methenyltetrahydrofolate cyclohydrolase
- Citrovorum factor cyclodehydrase
- cyclohydrolase
- formyl-methenyl-methylenetetrahydrofolate synthetase (combined)

comment:
In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate-tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.


entry: 3.5.4.12
sysname: dCMP aminohydrolase
comment: Also acts on some 5-substituted dCMPs.
reaction: dCMP + H2O = dUMP + NH3 [RN:R01663]
iubmb_reaction: R01663
kegg_reaction: R06137
name:
--- 
- dCMP deaminase
- deoxycytidylate deaminase
- deoxy-CMP-deaminase
- deoxycytidylate aminohydrolase
- deoxycytidine monophosphate deaminase
- deoxycytidine-5'-phosphate deaminase
- deoxycytidine-5'-monophosphate aminohydrolase


entry: 3.5.4.16
sysname: GTP 7,8-8,9-dihydrolase
iubmb_reaction: R00424
kegg_reaction: R00428 R04639 R05046 R05048
name:
--- 
- GTP cyclohydrolase I
- GTP cyclohydrolase
- guanosine triphosphate cyclohydrolase
- guanosine triphosphate 8-deformylase
- dihydroneopterin triphosphate synthase
- GTP 8-formylhydrolase

comment:
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic.

reaction:
GTP + 2 H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate [RN:R00424]


entry: 3.5.4.17
sysname: adenosine-phosphate aminohydrolase
reaction: 5'-AMP + H2O = 5'-IMP + NH3 [RN:R00181]
iubmb_reaction: R00181
kegg_reaction: R06137
name:
--- 
- adenosine-phosphate deaminase
- adenylate deaminase
- adenine nucleotide deaminase
- adenosine (phosphate) deaminase

comment:
Acts on 5'-AMP, ADP, ATP, NAD+ and adenosine, in decreasing order of activity. The bacterial enzyme also acts on the deoxy derivatives. cf. EC 3.5.4.6 AMP deaminase.


entry: 3.5.4.19
sysname: 1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase
iubmb_reaction: R04037
name:
--- 
- phosphoribosyl-AMP cyclohydrolase
- PRAMP-cyclohydrolase
- phosphoribosyladenosine monophosphate cyclohydrolase

comment:
The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).

reaction:
1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide [RN:R04037]


entry: 3.5.4.20
name: --- - pyrithiamine deaminase
iubmb_reaction: R04641
kegg_reaction: R06137
sysname:
1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methy lpyridinium-bromide aminohydrolase

reaction:
1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + H2O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + NH3 [RN:R04641]


entry: 3.5.4.23
name: --- - blasticidin-S deaminase
sysname: blasticidin-S aminohydrolase
reaction: blasticidin S + H2O = deaminohydroxyblasticidin S + NH3 [RN:R03800]
iubmb_reaction: R03800
kegg_reaction: R06137
comment:
Catalyses the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.


entry: 3.5.4.25
name: --- - GTP cyclohydrolase II - guanosine triphosphate cyclohydrolase II - GTP-8-formylhydrolase
sysname: GTP 7,8-8,9-dihydrolase (diphosphate-forming)
iubmb_reaction: R00425
comment:
Two C-N bonds are hydrolysed, releasing formate, with simultaneous removal of the terminal diphosphate.

reaction:
GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate [RN:R00425]


entry: 3.5.4.26
name: --- - diaminohydroxyphosphoribosylaminopyrimidine deaminase
sysname: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 2-aminohydrolase
comment: The substrate is the product of EC 3.5.4.25 GTP cyclohydrolase II.
iubmb_reaction: R03459
reaction:
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O = 5-amino-6-(5-phosphoribosylamino)uracil + NH3 [RN:R03459]


entry: 3.5.4.27
sysname: 5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing)
iubmb_reaction: R03464
name:
--- 
- methenyltetrahydromethanopterin cyclohydrolase
- 5,10-methenyltetrahydromethanopterin cyclohydrolase
- N5,N10-methenyltetrahydromethanopterin cyclohydrolase
- methenyl-H4MPT cyclohydrolase

comment:
Methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.

reaction:
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin [RN:R03464]


entry: 3.5.4.29
name: --- - GTP cyclohydrolase IIa
sysname: GTP 8,9-hydrolase (phosphate-forming)
iubmb_reaction: R07306
comment:
Requires Mg2+. This enzyme catalyses the hydrolysis of the imidazole ring of guanosine 5'-triphosphate, N7-methylguanosine 5'-triphosphate or inosine 5'-triphosphate. Xanthosine 5'-triphosphate and ATP are not substrates. It also catalyses the hydrolysis of diphosphate to form two equivalents of phosphate. Unlike GTP cyclohydrolase II (EC 3.5.4.25), this enzyme does not release formate, but does hydrolyze the diphosphate from GTP to phosphate.

reaction:
GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one + 2 phosphate [RN:R07306]


entry: 3.5.4.30
name: --- - dCTP deaminase (dUMP-forming)
sysname: dCTP aminohydrolase (dUMP-forming)
reaction: dCTP + 2 H2O = dUMP + diphosphate + NH3 [RN:R07307]
iubmb_reaction: R07307
comment:
Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly.


entry: 3.5.4.-
name: --- []
reaction:
(1) Cyromazine + H2O <=> N-Cyclopropylammeline + NH3 [RN:R06970]; (2) N-Cyclopropylammeline + H2O <=> N-Cyclopropylammelide + NH3 [RN:R06971]; (3) N-Cyclopropylammelide + H2O <=> Cyanuric acid + Cyclopropylamine [RN:R06972]


entry: 3.5.5.1
name: --- - nitrilase - acetonitrilase - benzonitrilase
sysname: nitrile aminohydrolase
reaction: A nitrile + 2 H2O = a carboxylate + NH3 [RN:R00540]
iubmb_reaction: R00540 > R01887 R03093 R03542 R05591
comment:
Acts on a wide range of aromatic nitriles including (indole-3-yl)acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides. cf. EC 4.2.1.84 nitrile hydratase.


entry: 3.5.5.5
name: --- - arylacetonitrilase
sysname: arylacetonitrile aminohydrolase
reaction: 4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3 [RN:R04140]
iubmb_reaction: R04140
kegg_reaction: R00540
comment:
Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.


entry: 3.5.5.7
name: --- - aliphatic nitrilase
sysname: aliphatic nitrile aminohydrolase
reaction: R-CN + 2 H2O = R-COOH + NH3 [RN:R00540]
iubmb_reaction: R00540 > R05358
comment:
preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 3.5.5.1). Substrates include crotononitrile, acrylonitrile and glutaronitrile.


entry: 3.5.99.2
name: --- - thiaminase - thiaminase II
sysname: thiamine hydrolase
iubmb_reaction: R02133
reaction:
thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole [RN:R02133]


entry: 3.5.99.3
name: --- - hydroxydechloroatrazine ethylaminohydrolase - AtzB - hydroxyatrazine ethylaminohydrolase
sysname: 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase
iubmb_reaction: R05559
kegg_reaction: R06966
comment:
Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria via N-isopropylammelide, 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine.

reaction:
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H2O = N-isopropylammelide + ethylamine [RN:R05559]


entry: 3.5.99.4
name: --- - N-isopropylammelide isopropylaminohydrolase - AtzC
sysname: N-isopropylammelide isopropylaminohydrolase
reaction: N-isopropylammelide + H2O = cyanuric acid + isopropylamine [RN:R05560]
iubmb_reaction: R05560
kegg_reaction: R06967
comment:
Involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopopylamino)-1,3,5-triazine, is degraded in bacteria via N-isopropylammelide, 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine.


entry: 3.5.99.5
name: --- - 2-aminomuconate deaminase
sysname: 2-aminomuconate aminohydrolase
reaction: 2-aminomuconate + H2O = 4-oxalocrotonate + NH3 [RN:R03887]
iubmb_reaction: R03887
comment:
Intermediate in the biodegradation of nitrobenzene by Pseudomonas pseudocaligenes JS45. The reaction is spontaneous in acid conditions.


entry: 3.5.99.6
sysname: 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
reaction: D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 [RN:R00765]
iubmb_reaction: R00765
name:
--- 
- glucosamine-6-phosphate deaminase
- glucosaminephosphate isomerase
- glucosamine-6-phosphate isomerase
- phosphoglucosaminisomerase
- glucosamine phosphate deaminase
- aminodeoxyglucosephosphate isomerase
- phosphoglucosamine isomerase

comment:
Formerly EC 5.3.1.10. Isomerization of the aldose-ketose type converts the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.


entry: 3.5.99.7
sysname: 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
reaction: 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3 [RN:R00997]
iubmb_reaction: R00997
name:
--- 
- 1-aminocyclopropane-1-carboxylate deaminase
- 1-aminocyclopropane-1-carboxylate endolyase (deaminating)

comment:
A pyridoxal 5'-phosphate enzyme. Its introduction has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.


entry: 3.5.99.-
name: --- []
reaction:
(1) 2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine + H2O <=> Cyanuric acid + Ethylamine [RN:R05573]; (2) Deisopropylhydroxyatrazine + H2O <=> 2,4-Dihydroxy-6-(N'-ethyl)amino-1,3,5-triazine + NH3 [RN:R05574]; (3) 2-Hydroxy-4,6-diamino-1,3,5-triazine + H2O <=> 2,4-Dihydroxy-6-amino-1,3,5-triazine + NH3 [RN:R06969]


entry: 3.6.1.1
name: --- - inorganic diphosphatase
sysname: diphosphate phosphohydrolase
reaction: diphosphate + H2O = 2 phosphate [RN:R00004]
iubmb_reaction: R00004
comment:
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form of this enzyme with a molecular mass of about 90 kDa is found in tonoplasts of plants and fungi, where it imports protons from the cytosol into the vacuolar lumen.


entry: 3.6.1.3
sysname: ATP phosphohydrolase
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- adenosinetriphosphatase
- adenylpyrophosphatase
- ATP monophosphatase
- triphosphatase
- ATPase
- SV40 T-antigen
- adenosine 5'-triphosphatase
- ATP hydrolase
- complex V (mitochondrial electron transport)
- (Ca2+ + Mg2+)-ATPase
- HCO3--ATPase
- adenosine triphosphatase

comment:
Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.


entry: 3.6.1.4
name: --- - Deleted entry
comment:
Deleted entry: adenosinetriphosphatase (Mg-activated). Now included with EC 3.6.1.3 adenosinetriphosphatase (EC 3.6.1.4 created 1961, deleted 1965)


entry: 3.6.1.5
sysname: ATP diphosphohydrolase (phosphate-forming)
reaction: ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
iubmb_reaction: R00085
kegg_reaction: R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
name:
--- 
- apyrase
- ATP-diphosphatase
- adenosine diphosphatase
- ADPase
- ATP diphosphohydrolase [ambiguous]

comment:
Requires Ca2+. Also acts on ADP, and on other nucleoside triphosphates and diphosphates. Most of the ecto-ATPases occurring on the cell surface and hydrolysing extracellular nucleoside triphosphates and diphosphates belong to this enzyme family. Either Ca2+ or Mg2+ can serve as activating ions.


entry: 3.6.1.6
sysname: nucleoside-diphosphate phosphohydrolase
comment: Acts on IDP, GDP, UDP and also on D-ribose 5-diphosphate
reaction: A nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
iubmb_reaction: R00329 > R00155 R00328 R00961
name:
--- 
- nucleoside-diphosphatase
- thiaminpyrophosphatase
- UDPase
- inosine diphosphatase
- adenosine diphosphatase
- IDPase
- ADPase
- adenosinepyrophosphatase
- guanosine diphosphatase
- guanosine 5'-diphosphatase
- inosine 5'-diphosphatase
- uridine diphosphatase
- uridine 5'-diphosphatase
- nucleoside diphosphate phosphatase
- type B nucleoside diphosphatase
- GDPase
- CDPase
- nucleoside 5'-diphosphatase
- type L nucleoside diphosphatase
- NDPase
- nucleoside diphosphate phosphohydrolase


entry: 3.6.1.7
sysname: acylphosphate phosphohydrolase
reaction: An acylphosphate + H2O = a carboxylate + phosphate [RN:R00539]
iubmb_reaction: R00539 > R00317 R01421 R01515
name:
--- 
- acylphosphatase
- acetylphosphatase
- 1,3-diphosphoglycerate phosphatase
- acetic phosphatase
- Ho 1-3
- GP 1-3


entry: 3.6.1.8
sysname: ATP diphosphohydrolase (diphosphate-forming)
comment: Also acts on ITP, GTP, CTP and UTP.
reaction: ATP + H2O = AMP + diphosphate [RN:R00087]
iubmb_reaction: R00087
kegg_reaction: R00086 R00287 R00426 R00515 R00662 R00720
name:
--- 
- ATP diphosphatase
- ATPase
- ATP pyrophosphatase
- adenosine triphosphate pyrophosphatase
- ATP diphosphohydrolase [ambiguous]


entry: 3.6.1.10
sysname: polyphosphate polyphosphohydrolase
comment: The product contains 4 or 5 phosphate residues.
reaction: polyphosphate + n H2O = (n+1) oligophosphate [RN:R00001]
iubmb_reaction: R00001
name:
--- 
- endopolyphosphatase
- polyphosphate depolymerase
- metaphosphatase
- polyphosphatase
- polymetaphosphatase


entry: 3.6.1.12
sysname: dCTP nucleotidohydrolase
comment: Also hydrolyses dCDP to dCMP and phosphate.
reaction: dCTP + H2O = dCMP + diphosphate [RN:R01668]
iubmb_reaction: R01668
kegg_reaction: R01667
name:
--- 
- dCTP diphosphatase
- deoxycytidine-triphosphatase
- dCTPase
- dCTP pyrophosphatase
- deoxycytidine triphosphatase
- deoxy-CTPase


entry: 3.6.1.13
sysname: ADP-ribose ribophosphohydrolase
reaction: ADP-ribose + H2O = AMP + D-ribose 5-phosphate [RN:R01054]
iubmb_reaction: R01054
name:
--- 
- ADP-ribose diphosphatase
- ADPribose pyrophosphatase
- adenosine diphosphoribose pyrophosphatase
- ADPR-PPase


entry: 3.6.1.14
name: --- - adenosine-tetraphosphatase
sysname: adenosine-tetraphosphate phosphohydrolase
reaction: adenosine 5'-tetraphosphate + H2O = ATP + phosphate [RN:R00128]
iubmb_reaction: R00128
kegg_reaction: R00723
comment:
Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates.


entry: 3.6.1.15
sysname: unspecific diphosphate phosphohydrolase
comment: Also hydrolyses other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD.
reaction: NTP + H2O = NDP + phosphate [RN:R02319]
iubmb_reaction: R02319 > R00086
kegg_reaction: R00615
name:
--- 
- nucleoside-triphosphatase
- nucleoside triphosphate phosphohydrolase
- nucleoside-5-triphosphate phosphohydrolase
- nucleoside 5-triphosphatase


entry: 3.6.1.16
sysname: CDP-glycerol phosphoglycerohydrolase
reaction: CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate [RN:R00855]
iubmb_reaction: R00855
name:
--- 
- CDP-glycerol diphosphatase
- CDP-glycerol pyrophosphatase
- cytidine diphosphoglycerol pyrophosphatase


entry: 3.6.1.17
sysname: P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase
reaction: P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
iubmb_reaction: R01232
kegg_reaction: R00184 R00969 R02805
name:
--- 
- bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)
- bis(5'-guanosyl)-tetraphosphatase
- bis(5'-adenosyl)-tetraphosphatase
- diguanosinetetraphosphatase (asymmetrical)
- dinucleosidetetraphosphatase (asymmetrical)
- diadenosine P1,P4-tetraphosphatase
- dinucleoside tetraphosphatase

comment:
Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate [cf. EC 3.6.1.41 bis(5'-nucleosyl)-tetraphosphatase (symmetrical)]


entry: 3.6.1.18
sysname: FAD nucleotidohydrolase
reaction: FAD + H2O = AMP + FMN [RN:R00160]
iubmb_reaction: R00160
name:
--- 
- FAD diphosphatase
- FAD pyrophosphatase
- riboflavin adenine dinucleotide pyrophosphatase
- flavin adenine dinucleotide pyrophosphatase
- riboflavine adenine dinucleotide pyrophosphatase
- flavine adenine dinucleotide pyrophosphatase

comment:
The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.


entry: 3.6.1.21
sysname: ADP-sugar sugarphosphohydrolase
comment: Has a specificity that is distinct from that of UDP-sugar diphosphatase (EC 3.6.1.45).
reaction: ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate [RN:R03570]
iubmb_reaction: R03570 > R00951 R01885 R02677
kegg_reaction: R00881 R01233
name:
--- 
- ADP-sugar diphosphatase
- ADP-sugar pyrophosphatase
- adenosine diphosphosugar pyrophosphatase


entry: 3.6.1.22
sysname: NAD+ phosphohydrolase
comment: Also acts on NADP+, 3-acetylpyridine and the thionicotinamide analogues of NAD+ and NADP+.
reaction: NAD+ + H2O = AMP + NMN [RN:R00103]
iubmb_reaction: R00103
kegg_reaction: R03004
name:
--- 
- NAD+ diphosphatase
- nicotinamide adenine dinucleotide pyrophosphatase
- NADP pyrophosphatase
- NADH pyrophosphatase


entry: 3.6.1.23
sysname: dUTP nucleotidohydrolase
reaction: dUTP + H2O = dUMP + diphosphate [RN:R02100]
iubmb_reaction: R02100
name:
--- 
- dUTP diphosphatase
- deoxyuridine-triphosphatase
- dUTPase
- dUTP pyrophosphatase
- desoxyuridine 5'-triphosphate nucleotidohydrolase
- desoxyuridine 5'-triphosphatase


entry: 3.6.1.26
sysname: CDP-diacylglycerol phosphatidylhydrolase
reaction: CDP-diacylglycerol + H2O = CMP + phosphatidate [RN:R01797]
iubmb_reaction: R01797
name:
--- 
- CDP-diacylglycerol diphosphatase
- cytidine diphosphodiacylglycerol pyrophosphatase
- CDP diacylglycerol hydrolase


entry: 3.6.1.27
sysname: undecaprenyl-diphosphate phosphohydrolase
reaction: undecaprenyl diphosphate + H2O = undecaprenyl phosphate + phosphate [RN:R05627]
iubmb_reaction: R05627
name:
--- 
- undecaprenyl-diphosphatase
- C55-isoprenyl diphosphatase
- C55-isoprenyl pyrophosphatase
- isoprenyl pyrophosphatase


entry: 3.6.1.29
sysname: P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase
reaction: P1-P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP [RN:R00187]
iubmb_reaction: R00187
kegg_reaction: R00186
name:
--- 
- bis(5'-adenosyl)-triphosphatase
- dinucleosidetriphosphatase
- diadenosine 5,5-P1,P3-triphosphatase


entry: 3.6.1.30
name: --- - m7G(5')pppN diphosphatase - decapase - m7G(5')pppN pyrophosphatase
sysname: 7-methylguanosine-5'-triphospho-5'-polynucleotide 7-methylguanosine-5'-phosphohydrolase
iubmb_reaction: R04368
reaction:
7-methylguanosine 5'-triphospho-5'-polynucleotide + H2O = 7-methylguanosine 5'-phosphate + polynucleotide [RN:R04368]


entry: 3.6.1.31
sysname: 1-(5-phosphoribosyl)-ATP diphosphohydrolase
reaction: 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate [RN:R04035]
iubmb_reaction: R04035
name:
--- 
- phosphoribosyl-ATP diphosphatase
- phosphoribosyl-ATP pyrophosphatase
- phosphoribosyladenosine triphosphate pyrophosphatase

comment:
The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase).


entry: 3.6.1.34
name: --- - Transferred to 3.6.3.14
comment:
transferred entry: now EC 3.6.3.14 H+-transporting two-sector ATPase (EC 3.6.1.34 created 1984, deleted 2000)


entry: 3.6.1.39
sysname: dTTP nucleotidohydrolase
comment: Also acts, more slowly, on dUTP and UTP.
reaction: dTTP + H2O = dTDP + phosphate [RN:R02095]
iubmb_reaction: R02095
kegg_reaction: R00159 R02330
name:
--- 
- thymidine-triphosphatase
- thymidine triphosphate nucleotidohydrolase
- dTTPase
- deoxythymidine-5'-triphosphatase


entry: 3.6.1.40
sysname: guanosine-5'-triphosphate,3'-diphosphate 5'-phosphohydrolase
iubmb_reaction: R03409
name:
--- 
- guanosine-5'-triphosphate,3'-diphosphate diphosphatase
- pppGpp 5'-phosphohydrolase
- guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
- guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase
- guanosine pentaphosphatase
- guanosine pentaphosphate phosphatase
- guanosine 5'-triphosphate 3'-diphosphate 5'-phosphatase
- guanosine pentaphosphate phosphohydrolase

comment:
Also hydrolyses other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate.

reaction:
guanosine 5'-triphosphate,3'-diphosphate + H2O = guanosine 5'-diphosphate,3'-diphosphate + phosphate [RN:R03409]


entry: 3.6.1.41
sysname: P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleosidebisphosphohydrolase
reaction: P1,P4-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP [RN:R00125]
iubmb_reaction: R00125
name:
--- 
- bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
- diadenosinetetraphosphatase (symmetrical)
- dinucleosidetetraphosphate (symmetrical)
- symmetrical diadenosine tetraphosphate hydrolase
- adenosine tetraphosphate phosphodiesterase
- Ap4A hydrolase
- bis(5'-adenosyl) tetraphosphatase
- diadenosine tetraphosphate hydrolase
- diadenosine polyphosphate hydrolase
- diadenosine 5',5'''-P1,P4-tetraphosphatase

comment:
Also acts on bis(5'-guanosyl) tetraphosphate and bis(5'-adenosyl) pentaphosphate and, more slowly, on some other polyphosphates, forming a nucleoside bisphosphate as one product in all cases [cf. EC 3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)].


entry: 3.6.1.43
sysname: dolichyl-diphosphate phosphohydrolase
reaction: dolichyl diphosphate + H2O = dolichyl phosphate + phosphate [RN:R01004]
iubmb_reaction: R01004
name:
--- 
- dolichyldiphosphatase
- dolichol diphosphatase
- dolichyl pyrophosphatase
- dolichyl pyrophosphate phosphatase
- dolichyl diphosphate phosphohydrolase
- Dol-P-P phosphohydrolase


entry: 3.6.1.44
sysname: oligosaccharide-diphosphodolichol phosphodolichohydrolase
iubmb_reaction: R04272
name:
--- 
- oligosaccharide-diphosphodolichol diphosphatase
- oligosaccharide-diphosphodolichol pyrophosphatase

reaction:
oligosaccharide-diphosphodolichol + H2O = oligosaccharide phosphate + dolichyl phosphate [RN:R04272]


entry: 3.6.1.45
sysname: UDP-sugar sugarphosphohydrolase
reaction: UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate [RN:R03986]
iubmb_reaction: R03986
name:
--- 
- UDP-sugar diphosphatase
- nucleosidediphosphate-sugar pyrophosphatase
- nucleosidediphosphate-sugar diphosphatase
- UDP-sugar hydrolase
- UDP-sugar pyrophosphatase

comment:
A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.


entry: 3.6.1.46
name: --- - Transferred to 3.6.5.1
comment:
Transferred entry: now EC 3.6.5.1 heterotrimeric G-protein GTPase. (EC 3.6.1.46 created 2000, deleted 2003)


entry: 3.6.1.48
name: --- - Transferred to 3.6.5.3
comment:
Transferred entry: now EC 3.6.5.3 protein-synthesizing GTPase. (EC 3.6.1.48 created 2000, deleted 200)


entry: 3.6.1.49
name: --- - Transferred to 3.6.5.4
comment:
Transferred entry: now EC 3.6.5.4 signal-recognition-particle GTPase. (EC 3.6.1.49 created 2000, deleted 2003)


entry: 3.6.1.52
sysname: diphospho-myo-inositol-polyphosphate diphosphohydrolase
reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate [RN:R05777]
iubmb_reaction: R05777 > R05779
name:
--- 
- diphosphoinositol-polyphosphate diphosphatase
- diphosphoinositol-polyphosphate phosphohydrolase
- DIPP

comment:
This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.


entry: 3.6.1.-
name: --- []
reaction:
(1) Isomaltose + ATP + H2O <=> Isomaltose + Orthophosphate + ADP [RN:R01719 R06220]; (2) UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + H2O <=> UMP + 2,3-Bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate [RN:R04549]; (3) 2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine + Orthophosphate <=> Dihydroneopterin phosphate + H2O [RN:R04621]; (4) 2-Amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate + H2O <=> Dihydroneopterin phosphate + Pyrophosphate [RN:R04638]; (5) Isomaltose + ATP + H2O <=> Isomaltose + Orthophosphate + ADP [RN:R06220]


entry: 3.6.2.1
sysname: adenylyl-sulfate sulfohydrolase
reaction: adenylyl sulfate + H2O = AMP + sulfate [RN:R00531]
iubmb_reaction: R00531
name:
--- 
- adenylylsulfatase
- adenosine 5-phosphosulfate sulfohydrolase
- adenylylsulfate sulfohydrolase


entry: 3.6.2.2
sysname: 3'-phosphoadenylyl-sulfate sulfohydrolase
comment: Requires Mn2+.
reaction: 3'-phosphoadenylyl sulfate + H2O = adenosine 3',5'-bisphosphate + sulfate [RN:R00507]
iubmb_reaction: R00507
name:
--- 
- phosphoadenylylsulfatase
- 3-phosphoadenylyl sulfatase
- 3-phosphoadenosine 5-phosphosulfate sulfatase
- PAPS sulfatase
- 3'-phosphoadenylylsulfate sulfohydrolase


entry: 3.6.3.1
sysname: ATP phosphohydrolase (phospholipid-flipping)
reaction: ATP + H2O + phospholipid(in) = ADP + phosphate + phospholipid(out) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- phospholipid-translocating ATPase
- Mg2+-ATPase
- flippase
- aminophospholipid-transporting ATPase

comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other ('flippase').


entry: 3.6.3.2
name: --- - Mg2+-importing ATPase
sysname: ATP phosphohydrolase (Mg2+-importing)
reaction: ATP + H2O + Mg2+(out) = ADP + phosphate + Mg2+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in both Gram-positive and Gram-negative bacteria, and three types are known, designated as CorA, MgtA and MgtB. The CorA itself is not an ATPase but an Mg2+ transporter.


entry: 3.6.3.3
name: --- - Cd2+-exporting ATPase
sysname: ATP phosphohydrolase (Cd2+-exporting)
reaction: ATP + H2O + Cd2+(in) = ADP + phosphate + Cd2+(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants.


entry: 3.6.3.4
name: --- - Cu2+-exporting ATPase
sysname: ATP phosphohydrolase (Cu2+-exporting)
reaction: ATP + H2O + Cu2+(in) = ADP + phosphate + Cu2+(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This bacterial and mammalian enzyme exports Cu2+ from cells. In humans, it is involved in Menkes disease and Wilson's disease.


entry: 3.6.3.5
name: --- - Zn2+-exporting ATPase - Zn(II)-translocating P-type ATPase - P1B-type ATPase - AtHMA4
sysname: ATP phosphohydrolase (Zn2+-exporting)
reaction: ATP + H2O + Zn2+(in) = ADP + phosphate + Zn2+(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme also exports Cd2+ and Pb2+.


entry: 3.6.3.6
sysname: ATP phosphohydrolase (H+-exporting)
reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- H+-exporting ATPase
- proton-translocating ATPase
- yeast plasma membrane H+-ATPase
- yeast plasma membrane ATPase
- ATP phosphohydrolase

comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.


entry: 3.6.3.7
name: --- - Na+-exporting ATPase
sysname: ATP phosphohydrolase (Na+-exporting)
reaction: ATP + H2O + Na+(in) = ADP + phosphate + Na+(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed.


entry: 3.6.3.8
sysname: ATP phosphohydrolase (Ca2+-transporting)
reaction: ATP + H2O + Ca2+(cis) = ADP + phosphate + Ca2+(trans) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- Ca2+-transporting ATPase
- sarcoplasmic reticulum ATPase
- sarco(endo)plasmic reticulum Ca2+-ATPase
- calcium pump
- Ca2+-pumping ATPase
- plasma membrane Ca-ATPase

comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in yeast. The first and third transport one ion per ATP hydrolysed, whereas the second transports two ions.


entry: 3.6.3.9
sysname: ATP phosphohydrolase (Na+/K+-exchanging)
reaction: ATP + H2O + Na+(in) + K+(out) = ADP + phosphate + Na+(out) + K+(in) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- Na+/K+-exchanging ATPase
- sodium pump
- Na+,K+ pump
- Na,K-pump
- (Na+ + K+)-activated ATPase
- (Na+ + K+)-ATPase
- Na+,K+-ATPase
- Na,K-activated ATPase

comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential.


entry: 3.6.3.10
name: --- - H+/K+-exchanging ATPase - H+-K+-ATPase - H,K-ATPase - (K+ + H+)-ATPase
sysname: ATP phosphohydrolase (H+/K+-exchanging)
reaction: ATP + H2O + H+(in) + K+(out) = ADP + phosphate + H+(out) + K+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A gastric mucosal enzyme that catalyses the efflux of one H+ and the influx of one K+ per ATP hydrolysed.


entry: 3.6.3.11
name: --- - Cl--transporting ATPase - Cl--translocating ATPase - Cl--motive ATPase
sysname: ATP phosphohydrolase (Cl--importing)
reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal and plant enzyme involved in the import of chloride anions.


entry: 3.6.3.12
name: --- - K+-transporting ATPase - K+-translocating Kdp-ATPase - multi-subunit K+-transport ATPase
sysname: ATP phosphohydrolase (K+-importing)
reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.


entry: 3.6.3.14
sysname: ATP phosphohydrolase (H+-transporting)
reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- H+-transporting two-sector ATPase
- ATP synthase
- F1-ATPase
- F(o)F1-ATPase
- H+-transporting ATPase
- mitochondrial ATPase
- coupling factors (F0, F1 and CF1)
- chloroplast ATPase
- bacterial Ca2+/Mg2+ ATPase

comment:
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archebacterial) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.


entry: 3.6.3.15
sysname: ATP phosphohydrolase (Na+-transporting)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- Na+-transporting two-sector ATPase
- ATP synthase
- vacuolar-type Na+-ATPase
- Na+-translocating ATPase
- Na+-translocating F1F(o)-ATPase
- vacuolar-type Na+-translocating ATPase

comment:
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+ replaces H+.


entry: 3.6.3.16
name: --- - arsenite-transporting ATPase
sysname: ATP phosphohydrolase (arsenite-exporting)
reaction: ATP + H2O + arsenite(in) = ADP + phosphate + arsenite(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. A bacterial enzyme that usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. Exports arsenite and antimonite anions.


entry: 3.6.3.17
name: --- - monosaccharide-transporting ATPase
sysname: ATP phosphohydrolase (monosaccharide-importing)
reaction: ATP + H2O + monosaccharide(out) = ADP + phosphate + monosaccharide(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Family of bacterial enzymes importing ribose, xylose, arabinose, galactose and methylgalactoside.


entry: 3.6.3.18
name: --- - oligosaccharide-transporting ATPase
sysname: ATP phosphohydrolase (disaccharide-importing)
reaction: ATP + H2O + oligosaccharide(out) = ADP + phosphate + oligosaccharide(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports lactose, melibiose and raffinose.


entry: 3.6.3.19
name: --- - maltose-transporting ATPase
sysname: ATP phosphohydrolase (maltose-importing)
reaction: ATP + H2O + maltose(out) = ADP + phosphate + maltose(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import maltose and maltose oligosaccharides.


entry: 3.6.3.20
name: --- - glycerol-3-phosphate-transporting ATPase
sysname: ATP phosphohydrolase (glycerol-3-phosphate-importing)
reaction: ATP + H2O + glycerol-3-phosphate(out) = ADP + phosphate + glycerol-3-phosphate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphorylated glycerol.


entry: 3.6.3.21
name: --- - polar-amino-acid-transporting ATPase - histidine permease
sysname: ATP phosphohydrolase (polar-amino-acid-importing)
reaction: ATP + H2O + polar amino acid(out) = ADP + phosphate + polar amino acid(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.


entry: 3.6.3.22
name: --- - nonpolar-amino-acid-transporting ATPase
sysname: ATP phosphohydrolase (nonpolar-amino-acid-transporting)
reaction: ATP + H2O + nonpolar amino acid(out) = ADP + phosphate + nonpolar amino acid(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import Leu, Ile and Val.


entry: 3.6.3.23
name: --- - oligopeptide-transporting ATPase - oligopeptide permease
sysname: ATP phosphohydrolase (oligopeptide-importing)
reaction: ATP + H2O + oligopeptide(out) = ADP + phosphate + oligopeptide(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports di- and oligopeptides.


entry: 3.6.3.24
name: --- - nickel-transporting ATPase
sysname: ATP phosphohydrolase (nickel-importing)
reaction: ATP + H2O + Ni2+(out) = ADP + phosphate + Ni2+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Ni2+.


entry: 3.6.3.25
name: --- - sulfate-transporting ATPase
sysname: ATP phosphohydrolase (sulfate-importing)
reaction: ATP + H2O + sulfate(out) = ADP + phosphate + sulfate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports sulfate and thiosulfate anions.


entry: 3.6.3.26
name: --- - nitrate-transporting ATPase
sysname: ATP phosphohydrolase (nitrate-importing)
reaction: ATP + H2O + nitrate(out) = ADP + phosphate + nitrate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports NO3-, NO2- and OCN-.


entry: 3.6.3.27
name: --- - phosphate-transporting ATPase - ABC phosphate transporter
sysname: ATP phosphohydrolase (phosphate-importing)
reaction: ATP + H2O + phosphate(out) = ADP + phosphate + phosphate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphate anions.


entry: 3.6.3.28
name: --- - phosphonate-transporting ATPase
sysname: ATP phosphohydrolase (phosphonate-transporting)
reaction: ATP + H2O + phosphonate(out) = ADP + phosphate + phosphonate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports phosphonate and organophosphate anions.


entry: 3.6.3.29
name: --- - molybdate-transporting ATPase
sysname: ATP phosphohydrolase (molybdate-importing)
reaction: ATP + H2O + molybdate(out) = ADP + phosphate + molybdate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports molybdate anions.


entry: 3.6.3.30
name: --- - Fe3+-transporting ATPase
sysname: ATP phosphohydrolase (ferric-ion-transporting)
reaction: ATP + H2O + Fe3+(out) = ADP + phosphate + Fe3+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports ferric cations.


entry: 3.6.3.31
name: --- - polyamine-transporting ATPase
sysname: ATP phosphohydrolase (polyamine-importing)
reaction: ATP + H2O + polyamine(out) = ADP + phosphate + polyamine(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine.


entry: 3.6.3.32
name: --- - quaternary-amine-transporting ATPase
sysname: ATP phosphohydrolase (quaternary-amine-importing)
reaction: ATP + H2O + quaternary amine(out) = ADP + phosphate + quaternary amine(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports betaine and glycine.


entry: 3.6.3.33
name: --- - vitamin B12-transporting ATPase
sysname: ATP phosphohydrolase (vitamin B12-importing)
reaction: ATP + H2O + vitamin B12(out) = ADP + phosphate + vitamin B12(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports cobalamin derivatives.


entry: 3.6.3.34
name: --- - iron-chelate-transporting ATPase
sysname: ATP phosphohydrolase (iron-chelate-importing)
reaction: ATP + H2O + iron chelate(out) = ADP + phosphate + iron chelate(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Fe-enterobactin, Fe-dicitrate, Fe-hydroxamate and other siderophores.


entry: 3.6.3.35
name: --- - manganese-transporting ATPase - ABC-type manganese permease complex
sysname: ATP phosphohydrolase (manganese-importing)
reaction: ATP + H2O + Mn2+(out) = ADP + phosphate + Mn2+(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports Mn2+, Zn2+ and iron chelates.


entry: 3.6.3.36
name: --- - taurine-transporting ATPase
sysname: ATP phosphohydrolase (taurine-importing)
reaction: ATP + H2O + taurine(out) = ADP + phosphate + taurine(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports taurine.


entry: 3.6.3.37
name: --- - guanine-transporting ATPase
sysname: ATP phosphohydrolase (guanine-importing)
reaction: ATP + H2O + guanine(out) = ADP + phosphate + guanine(in) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A eukaryotic enzyme that imports guanine and tryptophan (it contains a single ATP-binding site).


entry: 3.6.3.38
name: --- - capsular-polysaccharide-transporting ATPase
sysname: ATP phosphohydrolase (capsular-polysaccharide-exporting)
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide from Gram-negative bacteria.

reaction:
ATP + H2O + capsular polysaccharide(in) = ADP + phosphate + capsular polysaccharide(out) [RN:R00086]


entry: 3.6.3.39
name: --- - lipopolysaccharide-transporting ATPase
sysname: ATP phosphohydrolase (lipopolysaccharide-exporting)
reaction: ATP + H2O + lipopolysaccharide(in) = ADP + phosphate + lipopolysaccharide(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Enzymes of Gram-negative bacteria that export lipo-oligosaccharides and lipopolysaccharides.


entry: 3.6.3.40
name: --- - teichoic-acid-transporting ATPase
sysname: ATP phosphohydrolase (teichoic-acid-exporting)
reaction: ATP + H2O + teichoic acid(in) = ADP + phosphate + teichoic acid(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-positive bacteria that exports teichoic acid.


entry: 3.6.3.41
name: --- - heme-transporting ATPase
sysname: ATP phosphohydrolase (heme-exporting)
reaction: ATP + H2O + heme(in) = ADP + phosphate + heme(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports heme.


entry: 3.6.3.42
name: --- - beta-glucan-transporting ATPase
sysname: ATP phosphohydrolase (beta-glucan-exporting)
reaction: ATP + H2O + beta-glucan(in) = ADP + phosphate + beta-glucan(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports beta-glucan.


entry: 3.6.3.43
name: --- - peptide-transporting ATPase
sysname: ATP phosphohydrolase (peptide-exporting)
reaction: ATP + H2O + peptide(in) = ADP + phosphate + peptide(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A family of enzymes that exports alpha-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria.


entry: 3.6.3.44
sysname: ATP phosphohydrolase (xenobiotic-exporting)
reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out) [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- xenobiotic-transporting ATPase
- multidrug-resistance protein
- MDR protein
- P-glycoprotein
- pleiotropic-drug-resistance protein
- PDR protein
- steroid-transporting ATPase
- ATP phosphohydrolase (steroid-exporting)

comment:
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. The enzyme from Gram-positive bacteria and eukaryotic cells export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione-drug conjugates. Some also show some 'flippase' (phospholipid-translocating ATPase; EC 3.6.3.1) activity.


entry: 3.6.3.45
name: --- - Deleted entry
comment:
Deleted entry: steroid-transporting ATPase. Now included with EC 3.6.3.44, xenobiotic-transporting ATPase (EC 3.6.3.45 created 2000, deleted 2006)


entry: 3.6.3.46
name: --- - cadmium-transporting ATPase - yeast cadmium factor
sysname: ATP phosphohydrolase (heavy-metal-exporting)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.


entry: 3.6.3.47
name: --- - fatty-acyl-CoA-transporting ATPase
sysname: ATP phosphohydrolase (fatty-acyl-CoA-transporting)
reaction: ATP + H2O + fatty acyl CoA(cis) = ADP + phosphate + fatty acyl CoA(trans) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.


entry: 3.6.3.48
name: --- - alpha-factor-transporting ATPase
sysname: ATP phosphohydrolase (alpha-factor-transporting)
reaction: ATP + H2O + alpha-factor(in) = ADP + phosphate + alpha-factor(out) [RN:R00086]
iubmb_reaction: R00086
comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the alpha-factor sex pheromone.


entry: 3.6.3.49
sysname: ATP phosphohydrolase (channel-conductance-controlling)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
name:
--- 
- channel-conductance-controlling ATPase
- cystic-fibrosis membrane-conductance-regulating protein

comment:
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal enzyme that is active in forming a chloride channel, the absence of which brings about cystic fibrosis. It is also involved in the functioning of other transmembrane channels.


entry: 3.6.3.50
name: --- - protein-secreting ATPase
sysname: ATP phosphohydrolase (protein-secreting)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.


entry: 3.6.3.51
name: --- - mitochondrial protein-transporting ATPase
sysname: ATP phosphohydrolase (mitochondrial protein-importing)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. (TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.)


entry: 3.6.3.52
name: --- - chloroplast protein-transporting ATPase
sysname: ATP phosphohydrolase (chloroplast protein-importing)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).


entry: 3.6.3.53
name: --- - Ag+-exporting ATPase
sysname: ATP phosphohydrolase (Ag+-exporting)
reaction: ATP + H2O + Ag+(in) = ADP + phosphate + Ag+(out) [RN:R00086]
iubmb_reaction: R00086
comment:
A P-type ATPase that exports Ag+ ions from pathogenic microorganisms as well as from some animal tissues.


entry: 3.6.4.1
name: --- - myosin ATPase - actomyosin
sysname: ATP phosphohydrolase (actin-translocating)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.


entry: 3.6.4.2
name: --- - dynein ATPase
sysname: ATP phosphohydrolase (tubulin-translocating); dynein adenosine 5'-triphosphatase
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).


entry: 3.6.4.3
name: --- - microtubule-severing ATPase - katanin
sysname: ATP phosphohydrolase (tubulin-dimerizing)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.


entry: 3.6.4.4
name: --- - plus-end-directed kinesin ATPase - kinesin
sysname: kinesin ATP phosphohydrolase (plus-end-directed)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (alpha) chains (110 kDa) and two or more light (beta) chains (65-75 kDa). Also hydrolyses GTP.


entry: 3.6.4.5
name: --- - minus-end-directed kinesin ATPase
sysname: kinesin ATP phosphohydrolase (minus-end-directed)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Structurally almost identical to EC 3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules.


entry: 3.6.4.6
name: --- - vesicle-fusing ATPase
sysname: ATP phosphohydrolase (vesicle-fusing)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.


entry: 3.6.4.7
name: --- - peroxisome-assembly ATPase - peroxisome assembly factor-2
sysname: ATP phosphohydrolase (peroxisome-assembling)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa.


entry: 3.6.4.8
name: --- - proteasome ATPase - RP triple-A protein - RP triphosphatase
sysname: ATP phosphohydrolase (polypeptide-degrading)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Belongs to the AAA-type superfamily and, like EC 3.6.4.5 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.


entry: 3.6.4.9
name: --- - chaperonin ATPase - chaperonin
sysname: ATP phosphohydrolase (polypeptide-unfolding)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase).


entry: 3.6.4.10
name: --- - non-chaperonin molecular chaperone ATPase - molecular chaperone Hsc70 ATPase
sysname: ATP phosphohydrolase (polypeptide-polymerizing)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.


entry: 3.6.4.11
name: --- - nucleoplasmin ATPase
sysname: ATP phosphohydrolase (nucleosome-assembling)
reaction: ATP + H2O = ADP + phosphate [RN:R00086]
iubmb_reaction: R00086
comment:
An acidic nuclear protein that is active in the ATP-dependent assembly of nucleosome cores, in decondensation of sperm chromatin and in other histone-involving processes.


entry: 3.6.5.1
name: --- - heterotrimeric G-protein GTPase
sysname: GTP phosphohydrolase (signalling)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
comment:
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as G(s), G(i), G(o) and G(olf), targetting adenylate cyclase and/or K+ and Ca2+ channels; G(q) stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. G(olf) is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.


entry: 3.6.5.2
name: --- - small monomeric GTPase
sysname: GTP phosphohydrolase (cell-regulating)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
comment:
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).


entry: 3.6.5.3
sysname: GTP phosphohydrolase (mRNA-translation-assisting)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
name:
--- 
- protein-synthesizing GTPase
- elongation factor (EF)
- initiation factor (IF)
- peptide-release or termination factor

comment:
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.


entry: 3.6.5.4
name: --- - signal-recognition-particle GTPase
sysname: GTP phosphohydrolase (protein-synthesis-assisting)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
comment:
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).


entry: 3.6.5.5
name: --- - dynamin GTPase
sysname: GTP phosphohydrolase (vesicle-releasing)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
comment:
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.


entry: 3.6.5.6
name: --- - tubulin GTPase
sysname: GTP phosphohydrolase (microtubule-releasing)
reaction: GTP + H2O = GDP + phosphate [RN:R00335]
iubmb_reaction: R00335
comment:
An intrinsic activity of alpha-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.


entry: 3.7.1.3
name: --- - kynureninase
sysname: L-kynurenine hydrolase
reaction: L-kynurenine + H2O = anthranilate + L-alanine [RN:R00987]
iubmb_reaction: R00987
kegg_reaction: R02668 R03936
comment:
A pyridoxal-phosphate protein. Also acts on 3'-hydroxykynurenine and some other (3-arylcarbonyl)-alanines.


entry: 3.7.1.6
name: --- - acetylpyruvate hydrolase
sysname: 2,4-dioxopentanoate acetylhydrolase
reaction: acetylpyruvate + H2O = acetate + pyruvate [RN:R00324]
iubmb_reaction: R00324
comment:
Highly specific; does not act on pyruvate, oxaloacetate, maleylpyruvate, fumarylpyruvate or acetylacetone.


entry: 3.7.1.7
name: --- - beta-diketone hydrolase - oxidized PVA hydrolase
sysname: nonane-4,6-dione acylhydrolase
reaction: nonane-4,6-dione + H2O = pentan-2-one + butanoate [RN:R03781]
iubmb_reaction: R03781
comment:
Also acts on the product of the action of EC 1.1.3.18 secondary-alcohol oxidase, on polyvinyl alcohols; involved in the bacterial degradation of polyvinyl alcohol.


entry: 3.7.1.8
name: --- - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase - HOHPDA hydrolase
sysname: 2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase
reaction: 2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate [RN:R02606]
iubmb_reaction: R02606
kegg_reaction: R05359 R05360 R05361
comment:
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.


entry: 3.7.1.9
sysname: 2-hydroxymuconate-semialdehyde formylhydrolase
reaction: 2-hydroxymuconate semialdehyde + H2O = formate + 2-oxopent-4-enoate [RN:R02604]
iubmb_reaction: R02604
kegg_reaction: R05296 R05362 R05865
name:
--- 
- 2-hydroxymuconate-semialdehyde hydrolase
- 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase
- 2-hydroxymuconic semialdehyde hydrolase
- HMSH
- HOD hydrolase


entry: 3.7.1.10
name: --- - cyclohexane-1,3-dione hydrolase - 1,3-cyclohexanedione hydrolase
sysname: cyclohexane-1,3-dione acylhydrolase (decyclizing)
reaction: cyclohexane-1,3-dione + H2O = 5-oxohexanoate [RN:R03211]
iubmb_reaction: R03211
comment:
Highly specific; does not act on other dione derivatives of cyclohexane, cyclopentane or cycloheptane.


entry: 3.7.1.-
name: --- []
reaction:
(1) Glycolate + Pyruvate <=> (4S)-5-Hydroxy-2,4-dioxopentanoate + H2O [RN:R01335]; (2) 2-Hydroxy-2,4-pentadienoate + Succinate <=> 2-Hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O [RN:R02603]; (3) 4-Carboxy-2-hydroxymuconate semialdehyde + H2O <=> 4-Carboxy-2-oxo-4-pentanoate + Formate [RN:R04488]; (4) Adipate semialdehyde <=> Cyclohexan-1,2-dione + H2O [RN:R05100]; (5) 2-Hydroxy-2,4-pentadienoate + Acetate <=> 2-Hydroxy-6-keto-2,4-heptadienoate + H2O [RN:R05138]; (6) 6-Oxo-2-hydroxy-7-(4'-chlorophenyl)-3,8,8-trichloroocta-2E,4E,7E- trienoate + H2O <=> 2-(4'-Chlorophenyl)-3,3-dichloropropenoate + 2-Hydroxy-3-chloropenta-2,4-dienoate [RN:R05363]; (7) 2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O <=> 2-Methylpropanoate + 2-Hydroxy-2,4-pentadienoate [RN:R05364]; (8) 2-Hydroxy-6-oxo-(2'-aminophenyl)-hexa-2,4-dienoate + H2O <=> 2-Hydroxy-2,4-pentadienoate + Anthranilate [RN:R05365]; (9) 2-Hydroxy-6-oxo-octa-2,4-dienoate + H2O <=> 2-Hydroxy-2,4-pentadienoate + Propanoate + H+ [RN:R05366]; (10) 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA + 2 H2O <=> 3-Hydroxypimeloyl-CoA [RN:R05594]; (11) 4-Isopropenyl-2-oxy-cyclohexanecarboxyl-CoA + H2O <=> 3-Isopropenylpimelyl-CoA [RN:R06371]; (12) 2-Hydroxy-6-ketononatrienedioate + H2O <=> 2-Hydroxy-2,4-pentadienoate + Fumarate [RN:R06789]


entry: 3.8.1.2
sysname: (S)-2-haloacid halidohydrolase
reaction: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R03830]
iubmb_reaction: R03830 > R05287
name:
--- 
- (S)-2-haloacid dehalogenase
- 2-haloacid dehalogenase[ambiguous]
- 2-haloacid halidohydrolase [ambiguous][ambiguous]
- 2-haloalkanoic acid dehalogenase
- 2-haloalkanoid acid halidohydrolase
- 2-halocarboxylic acid dehalogenase II
- DL-2-haloacid dehalogenase[ambiguous]
- L-2-haloacid dehalogenase
- L-DEX

comment:
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]


entry: 3.8.1.6
name: --- - 4-chlorobenzoate dehalogenase - halobenzoate dehalogenase
sysname: 4-chlorobenzoate chlorohydrolase
reaction: 4-chlorobenzoate + H2O = 4-hydroxybenzoate + chloride [RN:R01307]
iubmb_reaction: R01307
comment:
Catalyses the first step in the degradation of chlorobenzoate in Pseudomonas. In many microorganisms, this activity comprises three separate enzymes, EC 6.2.1.33 (4-chlorobenzoate-CoA ligase), EC 3.8.1.7 (4-chlorobenzoyl-CoA dehalogenase) and EC 3.1.2.23 (4-hydroxybenzoyl-CoA thioesterase).


entry: 3.8.1.7
name: --- - 4-chlorobenzoyl-CoA dehalogenase
sysname: 4-chlorobenzoyl CoA chlorohydrolase
reaction: 4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride [RN:R04101]
iubmb_reaction: R04101
comment:
specific for dehalogenation at the 4-position. Can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position. This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.


entry: 3.8.1.8
name: --- - atrazine chlorohydrolase - AtzA
sysname: atrazine chlorohydrolase
reaction: atrazine + H2O = 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl [RN:R05558]
iubmb_reaction: R05558
comment:
Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.


entry: 3.8.1.9
sysname: (R)-2-haloacid halidohydrolase
reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07308]
iubmb_reaction: R07308
name:
--- 
- (R)-2-haloacid dehalogenase
- 2-haloalkanoic acid dehalogenase[ambiguous]
- 2-haloalkanoid acid halidohydrolase[ambiguous]
- D-2-haloacid dehalogenase
- D-DEX

comment:
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]


entry: 3.8.1.10
sysname: (R,S)-2-haloacid dehalogenase (configuration-inverting)
iubmb_reaction: R03830 R07308
name:
--- 
- 2-haloacid dehalogenase (configuration-inverting)
- 2-haloalkanoic acid dehalogenase
- 2-haloalkanoid acid halidohydrolase
- DL-2-haloacid dehalogenase
- DL-2-haloacid dehalogenase (inversion of configuration)
- DL-2-haloacid halidohydrolase (inversion of configuration)
- DL-DEXi

comment:
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]

reaction:
(1) (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R03830]; (2) (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07308]


entry: 3.8.1.11
sysname: (R,S)-2-haloacid dehalogenase (configuration-retaining)
iubmb_reaction: R07309 R07310
name:
--- 
- 2-haloacid dehalogenase (configuration-retaining)
- 2-haloalkanoic acid dehalogenase
- 2-haloalkanoid acid halidohydrolase
- DL-2-haloacid dehalogenase
- DL-DEXr

comment:
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (S)- and (R)-hydroxyalkanoic acids, respectively, with retention of configuration at C-2. [See also EC 3.8.1.2 (S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting)]

reaction:
(1) (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide [RN:R07309]; (2) (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide [RN:R07310]


entry: 3.8.1.-
name: --- []
reaction:
(1) trans-3-Chloroacrylic acid + H2O <=> HCl + 3-Oxopropanoate [RN:R05371]; (2) cis-3-Chloroacrylic acid + H2O <=> HCl + 3-Oxopropanoate [RN:R05372]; (3) Deisopropylatrazine + H2O <=> Deisopropylhydroxyatrazine + HCl [RN:R05572]


entry: 3.8.2.1
name: --- - Transferred to 3.1.8.2
comment:
Transferred entry: diisopropyl-fluorophosphatase. Now listed as EC 3.1.8.2 diisopropyl-fluorophosphatase (EC 3.8.2.1 created 1961, modified 1976, deleted 1992)


entry: 3.9.1.1
name: --- - phosphoamidase - creatine phosphatase
sysname: phosphamide hydrolase
reaction: N-phosphocreatine + H2O = creatine + phosphate [RN:R01882]
iubmb_reaction: R01882
comment:
Also acts on N-phospho-arginine and other phosphoamides. Possibly identical with EC 3.1.3.9 (glucose-6-phosphatase) or EC 3.1.3.16 (phosphoprotein phosphatase).


entry: 3.10.1.1
sysname: N-sulfo-D-glucosamine sulfohydrolase
reaction: N-sulfo-D-glucosamine + H2O = D-glucosamine + sulfate [RN:R01963]
iubmb_reaction: R01963
name:
--- 
- N-sulfoglucosamine sulfohydrolase
- sulfoglucosamine sulfamidase
- heparin sulfamidase
- 2-desoxy-D-glucoside-2-sulphamate sulphohydrolase (sulphamate sulphohydrolase)


entry: 3.10.1.2
sysname: cyclohexylsulfamate sulfohydrolase
comment: Also readily hydrolyses aliphatic sulfamates with 3 to 8 carbons.
reaction: cyclohexylsulfamate + H2O = cyclohexylamine + sulfate [RN:R02564]
iubmb_reaction: R02564
name:
--- 
- cyclamate sulfohydrolase
- cyclamate sulfamatase
- cyclamate sulfamidase
- cyclohexylsulfamate sulfamidase


entry: 3.11.1.1
sysname: 2-oxoethylphosphonate phosphonohydrolase
reaction: phosphonoacetaldehyde + H2O = acetaldehyde + phosphate [RN:R00747]
iubmb_reaction: R00747
name:
--- 
- phosphonoacetaldehyde hydrolase
- phosphonatase
- 2-phosphonoacetylaldehyde phosphonohydrolase

comment:
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond.


entry: 3.13.1.1
sysname: UDP-6-sulfo-6-deoxyglucose sulfohydrolase
reaction: UDP-glucose + sulfite = UDP-6-sulfoquinovose + H2O [RN:R05775]
iubmb_reaction: R05775
name:
--- 
- UDP-sulfoquinovose synthase
- sulfite:UDP-glucose sulfotransferase
- UDPsulfoquinovose synthase

comment:
Requires NAD+, which appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add; the reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.


entry: 3.13.1.2
name: --- - Deleted entry
comment:
Deleted entry: 5-deoxyribos-5-ylhomocysteinase. The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase. (EC 3.13.1.2 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: 3.13.1.3
sysname: 2'-hydroxybiphenyl-2-sulfinate sulfohydrolase
reaction: 2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite [RN:R07311]
iubmb_reaction: R07311
name:
--- 
- 2'-hydroxybiphenyl-2-sulfinate desulfinase
- gene dszB-encoded hydrolase
- 2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase
- DszB
- HBPSi desulfinase
- 2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase
- HPBS desulfinase
- 2-(2-hydroxyphenyl)benzenesulfinate hydrolase
- 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase
- 2-(2-hydroxyphenyl)benzenesulfinate desulfinase

comment:
The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date [2].


entry: 4.1.1.1
sysname: 2-oxo-acid carboxy-lyase
comment: A thiamine-diphosphate protein. Also catalyses acyloin formation.
reaction: A 2-oxo acid = an aldehyde + CO2 [RN:R00636]
iubmb_reaction: R00636 > R00224
kegg_reaction: R00014 R00755
name:
--- 
- pyruvate decarboxylase
- alpha-carboxylase
- pyruvic decarboxylase
- alpha-ketoacid carboxylase


entry: 4.1.1.2
name: --- - oxalate decarboxylase
sysname: oxalate carboxy-lyase
reaction: oxalate + H+ = formate + CO2 [RN:R00522]
iubmb_reaction: R00522
comment:
The enzyme from Bacillus subtilis contains manganese and requires O2 for activity, even though there is no net redox change.


entry: 4.1.1.3
sysname: oxaloacetate carboxy-lyase
reaction: oxaloacetate = pyruvate + CO2 [RN:R00217]
iubmb_reaction: R00217
kegg_reaction: R00214 R00216 R00471
name:
--- 
- oxaloacetate decarboxylase
- oxaloacetate beta-decarboxylase
- oxalacetic acid decarboxylase
- oxalate beta-decarboxylase

comment:
The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+.


entry: 4.1.1.9
name: --- - malonyl-CoA decarboxylase - malonyl coenzyme A decarboxylase
sysname: malonyl-CoA carboxy-lyase
reaction: malonyl-CoA = acetyl-CoA + CO2 [RN:R00233]
iubmb_reaction: R00233
kegg_reaction: R05373
comment:
Specific for malonyl-CoA. The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 2.8.3.3 malonate CoA-transferase.


entry: 4.1.1.10
name: --- - Deleted entry
comment:
Deleted entry: formerly aminomalonate decarboxylase. Now included with EC 4.1.1.12 aspartate 4-decarboxylase (EC 4.1.1.10 created 1961, deleted 1972)


entry: 4.1.1.11
sysname: L-aspartate 1-carboxy-lyase
comment: The Escherichia coli enzyme contains a pyruvoyl group.
reaction: L-aspartate = beta-alanine + CO2 [RN:R00489]
iubmb_reaction: R00489
name:
--- 
- aspartate 1-decarboxylase
- aspartate alpha-decarboxylase
- L-aspartate alpha-decarboxylase
- aspartic alpha-decarboxylase


entry: 4.1.1.12
sysname: L-aspartate 4-carboxy-lyase
reaction: L-aspartate = L-alanine + CO2 [RN:R00397]
iubmb_reaction: R00397
kegg_reaction: R00863
name:
--- 
- aspartate 4-decarboxylase
- desulfinase
- aminomalonic decarboxylase
- aspartate beta-decarboxylase
- aspartate omega-decarboxylase
- aspartic omega-decarboxylase
- aspartic beta-decarboxylase
- L-aspartate beta-decarboxylase
- cysteine sulfinic desulfinase
- L-cysteine sulfinate acid desulfinase

comment:
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.


entry: 4.1.1.15
sysname: L-glutamate 1-carboxy-lyase
reaction: L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
iubmb_reaction: R00261
kegg_reaction: R00489 R01682 R02466
name:
--- 
- glutamate decarboxylase
- L-glutamic acid decarboxylase
- L-glutamic decarboxylase
- cysteic acid decarboxylase
- L-glutamate alpha-decarboxylase
- aspartate 1-decarboxylase
- aspartic alpha-decarboxylase
- L-aspartate-alpha-decarboxylase
- gamma-glutamate decarboxylase

comment:
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.


entry: 4.1.1.20
sysname: meso-2,6-diaminoheptanedioate carboxy-lyase
comment: A pyridoxal-phosphate protein.
reaction: meso-2,6-diaminoheptanedioate = L-lysine + CO2 [RN:R00451]
iubmb_reaction: R00451
name:
--- 
- diaminopimelate decarboxylase
- diaminopimelic acid decarboxylase
- meso-diaminopimelate decarboxylase
- DAP-decarboxylase


entry: 4.1.1.21
sysname: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
iubmb_reaction: R04209
name:
--- 
- phosphoribosylaminoimidazole carboxylase
- 5-phosphoribosyl-5-aminoimidazole carboxylase
- 5-amino-1-ribosylimidazole 5-phosphate carboxylase
- AIR carboxylase
- 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase
- ADE2

comment:
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.

reaction:
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2 [RN:R04209]


entry: 4.1.1.22
name: --- - histidine decarboxylase - L-histidine decarboxylase
sysname: L-histidine carboxy-lyase
reaction: L-histidine = histamine + CO2 [RN:R01167]
iubmb_reaction: R01167
comment:
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.


entry: 4.1.1.23
sysname: orotidine-5'-phosphate carboxy-lyase
comment: The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
reaction: orotidine 5'-phosphate = UMP + CO2 [RN:R00965]
iubmb_reaction: R00965
name:
--- 
- orotidine-5'-phosphate decarboxylase
- orotidine-5'-monophosphate decarboxylase
- orotodylate decarboxylase
- orotidine phosphate decarboxylase
- OMP decarboxylase
- orotate monophosphate decarboxylase
- orotidine monophosphate decarboxylase
- OMP-DC
- orotate decarboxylase
- orotidine 5'-phosphate decarboxylase
- orotidylic decarboxylase
- orotidylic acid decarboxylase
- ODCase
- orotic decarboxylase


entry: 4.1.1.25
name: --- - tyrosine decarboxylase - L-tyrosine decarboxylase - L-(-)-tyrosine apodecarboxylase
sysname: L-tyrosine carboxy-lyase
reaction: L-tyrosine = tyramine + CO2 [RN:R00736]
iubmb_reaction: R00736
kegg_reaction: R02080
comment:
A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.


entry: 4.1.1.26
name: --- - Deleted entry
comment:
Deleted entry: DOPA decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase (EC 4.1.1.26 created 1961, deleted 1972)


entry: 4.1.1.27
name: --- - Deleted entry
comment:
Deleted entry: tryptophan decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase (EC 4.1.1.27 created 1961, deleted 1972)


entry: 4.1.1.28
sysname: aromatic-L-amino-acid carboxy-lyase
iubmb_reaction: R02080 R02701
kegg_reaction: R00685 R00699 R00736 R01167 R04909
name:
--- 
- aromatic-L-amino-acid decarboxylase
- DOPA decarboxylase
- tryptophan decarboxylase
- hydroxytryptophan decarboxylase
- L-DOPA decarboxylase
- aromatic amino acid decarboxylase
- 5-hydroxytryptophan decarboxylase

comment:
A pyridoxal-phosphate protein. The enzyme acts on L-tryptophan, 5-hydroxy-L-tryptophan and dihydroxy-L-phenylalanine.

reaction:
(1) 3,4-dihydroxy-L-phenylalanine = dopamine + CO2 [RN:R02080]; (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2 [RN:R02701]


entry: 4.1.1.29
sysname: 3-sulfino-L-alanine carboxy-lyase
reaction: 3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
iubmb_reaction: R02466
kegg_reaction: R01682
name:
--- 
- sulfinoalanine decarboxylase
- cysteine-sulfinate decarboxylase
- L-cysteinesulfinic acid decarboxylase
- CADCase/CSADCase
- CSAD
- cysteic decarboxylase
- cysteinesulfinic acid decarboxylase
- cysteinesulfinate decarboxylase
- sulfoalanine decarboxylase

comment:
A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme.


entry: 4.1.1.31
sysname: phosphate:oxaloacetate carboxy-lyase (phosphorylating)
reaction: phosphate + oxaloacetate = H2O + phosphoenolpyruvate + CO2 [RN:R00345]
iubmb_reaction: R00345
name:
--- 
- phosphoenolpyruvate carboxylase
- phosphopyruvate (phosphate) carboxylase
- PEP carboxylase
- phosphoenolpyruvic carboxylase
- PEPC
- PEPCase


entry: 4.1.1.32
sysname: GTP:oxaloacetate carboxy-lyase (transphosphorylating)
comment: ITP can act as phosphate donor.
reaction: GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 [RN:R00431]
iubmb_reaction: R00431
kegg_reaction: R00726
name:
--- 
- phosphoenolpyruvate carboxykinase (GTP)
- phosphoenolpyruvate carboxylase
- phosphopyruvate carboxylase
- phosphopyruvate (guanosine triphosphate) carboxykinase
- phosphoenolpyruvic carboxykinase (GTP)
- phosphopyruvate carboxylase (GTP)
- phosphoenolpyruvic carboxylase (GTP)
- phosphoenolpyruvic carboxykinase
- phosphoenolpyruvate carboxykinase
- PEP carboxylase


entry: 4.1.1.33
sysname: ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating)
reaction: ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2 [RN:R01121]
iubmb_reaction: R01121
name:
--- 
- diphosphomevalonate decarboxylase
- pyrophosphomevalonate decarboxylase
- mevalonate-5-pyrophosphate decarboxylase
- pyrophosphomevalonic acid decarboxylase
- 5-pyrophosphomevalonate decarboxylase
- mevalonate 5-diphosphate decarboxylase


entry: 4.1.1.34
sysname: 3-dehydro-L-gulonate carboxy-lyase
reaction: 3-dehydro-L-gulonate = L-xylulose + CO2 [RN:R01905]
iubmb_reaction: R01905
name:
--- 
- dehydro-L-gulonate decarboxylase
- keto-L-gulonate decarboxylase
- 3-keto-L-gulonate decarboxylase


entry: 4.1.1.36
sysname: N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase
reaction: N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2 [RN:R03269]
iubmb_reaction: R03269
name:
--- 
- phosphopantothenoylcysteine decarboxylase
- 4-phosphopantotheoylcysteine decarboxylase
- 4-phosphopantothenoyl-L-cysteine decarboxylase
- PPC-decarboxylase


entry: 4.1.1.37
sysname: uroporphyrinogen-III carboxy-lyase
comment: Acts on a number of porphyrinogens.
reaction: uroporphyrinogen III = coproporphyrinogen III + 4 CO2 [RN:R03197]
iubmb_reaction: R03197
kegg_reaction: R04972
name:
--- 
- uroporphyrinogen decarboxylase
- uroporphyrinogen III decarboxylase
- porphyrinogen carboxy-lyase
- porphyrinogen decarboxylase


entry: 4.1.1.38
sysname: diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)
comment: Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
reaction: diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2 [RN:R00346]
iubmb_reaction: R00346
name:
--- 
- phosphoenolpyruvate carboxykinase (diphosphate)
- phosphopyruvate carboxylase
- phosphoenolpyruvate carboxylase
- PEP carboxyphosphotransferase
- PEP carboxykinase
- phosphopyruvate carboxykinase (pyrophosphate)
- PEP carboxylase
- phosphopyruvate carboxykinase
- phosphoenolpyruvic carboxykinase
- phosphoenolpyruvic carboxylase
- phosphoenolpyruvate carboxykinase
- phosphoenolpyruvate carboxytransphosphorylase
- PEPCTrP
- phosphoenolpyruvic carboxykinase (pyrophosphate)
- phosphoenolpyruvic carboxylase (pyrophosphate)
- phosphoenolpyruvate carboxyphosphotransferase
- phosphoenolpyruvic carboxytransphosphorylase
- phosphoenolpyruvate carboxylase (pyrophosphate)
- phosphopyruvate carboxylase (pyrophosphate)


entry: 4.1.1.39
sysname: 3-phospho-D-glycerate carboxy-lyase (dimerizing)
comment: Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and 2-phosphoglycolate.
reaction: D-ribulose 1,5-bisphosphate + CO2 + H2O = 2 3-phospho-D-glycerate + 2 H+ [RN:R00024]
iubmb_reaction: R00024
kegg_reaction: R03140
name:
--- 
- ribulose-bisphosphate carboxylase
- D-ribulose 1,5-diphosphate carboxylase
- D-ribulose-1,5-bisphosphate carboxylase
- RuBP carboxylase
- carboxydismutase
- diphosphoribulose carboxylase
- ribulose 1,5-bisphosphate carboxylase
- ribulose 1,5-bisphosphate carboxylase/oxygenase
- ribulose 1,5-diphosphate carboxylase
- ribulose 1,5-diphosphate carboxylase/oxygenase
- ribulose bisphosphate carboxylase/oxygenase
- ribulose diphosphate carboxylase
- ribulose diphosphate carboxylase/oxygenase
- rubisco


entry: 4.1.1.41
sysname: (S)-methylmalonyl-CoA carboxy-lyase
reaction: (S)-methylmalonyl-CoA = propanoyl-CoA + CO2 [RN:R00923]
iubmb_reaction: R00923
name:
--- 
- methylmalonyl-CoA decarboxylase
- propionyl-CoA carboxylase
- propionyl coenzyme A carboxylase
- methylmalonyl-coenzyme A decarboxylase
- (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect]

comment:
The enzyme from Veillonella alcalescens is a biotinyl-protein, requires Na+ and acts as a sodium pump.


entry: 4.1.1.45
sysname: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
comment: Product rearranges non-enzymically to picolinate.
reaction: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2 [RN:R04323]
iubmb_reaction: R04323
name:
--- 
- aminocarboxymuconate-semialdehyde decarboxylase
- picolinic acid carboxylase
- picolinic acid decarboxylase
- alpha-amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase
- alpha-amino-beta-carboxymuconate-epsilon-semialdehyde beta-decarboxylase
- 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase


entry: 4.1.1.47
sysname: glyoxylate carboxy-lyase (dimerizing)
comment: A flavoprotein.
reaction: 2 glyoxylate = tartronate semialdehyde + CO2 [RN:R00013]
iubmb_reaction: R00013
name:
--- 
- tartronate-semialdehyde synthase
- tartronate semialdehyde carboxylase
- glyoxylate carbo-ligase
- glyoxylic carbo-ligase
- hydroxymalonic semialdehyde carboxylase
- tartronic semialdehyde carboxylase
- glyoxalate carboligase


entry: 4.1.1.48
iubmb_reaction: R03508
name:
--- 
- indole-3-glycerol-phosphate synthase
- indoleglycerol phosphate synthetase
- indoleglycerol phosphate synthase
- indole-3-glycerophosphate synthase

sysname:
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing; 1-C-(indol-3-yl)glycerol 3-phosphate-forming]

comment:
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].

reaction:
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O [RN:R03508]


entry: 4.1.1.49
sysname: ATP:oxaloacetate carboxy-lyase (transphosphorylating)
reaction: ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2 [RN:R00341]
iubmb_reaction: R00341
name:
--- 
- phosphoenolpyruvate carboxykinase (ATP)
- phosphopyruvate carboxylase (ATP)
- phosphoenolpyruvate carboxylase
- phosphoenolpyruvate carboxykinase
- phosphopyruvate carboxykinase (adenosine triphosphate)
- PEP carboxylase
- PEP carboxykinase
- PEPCK (ATP)
- PEPK
- PEPCK
- phosphoenolpyruvic carboxylase
- phosphoenolpyruvic carboxykinase
- phosphoenolpyruvate carboxylase (ATP)
- phosphopyruvate carboxykinase


entry: 4.1.1.50
sysname: S-adenosyl-L-methionine carboxy-lyase
comment: The Escherichia coli enzyme contains a pyruvoyl group.
reaction: S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2 [RN:R00178]
iubmb_reaction: R00178
name:
--- 
- adenosylmethionine decarboxylase
- S-adenosylmethionine decarboxylase
- S-adenosyl-L-methionine decarboxylase


entry: 4.1.1.51
name: --- - 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase
sysname: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase
iubmb_reaction: R03461
reaction:
3-hydroxy-2-methylpyridine-4,5-dicarboxylate = 3-hydroxy-2-methylpyridine-5-carboxylate + CO2 [RN:R03461]


entry: 4.1.1.52
sysname: 6-methylsalicylate carboxy-lyase
reaction: 6-methylsalicylate = 3-cresol + CO2 [RN:R03567]
iubmb_reaction: R03567
name:
--- 
- 6-methylsalicylate decarboxylase
- 6-methylsalicylic acid (2,6-cresotic acid) decarboxylase
- 6-MSA decarboxylase


entry: 4.1.1.53
sysname: L-phenylalanine carboxy-lyase
comment: A pyridoxal-phosphate protein. Also acts on tyrosine and other aromatic amino acids.
reaction: L-phenylalanine = phenylethylamine + CO2 [RN:R00699]
iubmb_reaction: R00699
name:
--- 
- phenylalanine decarboxylase
- L-phenylalanine decarboxylase
- aromatic L-amino acid decarboxylase


entry: 4.1.1.64
sysname: 2,2-dialkylglycine carboxy-lyase (amino-transferring)
reaction: 2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine [RN:R03854]
iubmb_reaction: R03854
name:
--- 
- 2,2-dialkylglycine decarboxylase (pyruvate)
- dialkyl amino acid (pyruvate) decarboxylase
- alpha-dialkyl amino acid transaminase
- 2,2-dialkyl-2-amino acid-pyruvate aminotransferase
- L-alanine-alpha-ketobutyrate aminotransferase
- dialkylamino-acid decarboxylase (pyruvate)

comment:
A pyridoxal-phosphate protein. Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate.


entry: 4.1.1.67
sysname: UDP-D-galacturonate carboxy-lyase
reaction: UDP-D-galacturonate = UDP-L-arabinose + CO2 [RN:R02636]
iubmb_reaction: R02636
name:
--- 
- UDP-galacturonate decarboxylase
- UDP-galacturonic acid decarboxylase
- UDPGalUA carboxy lyase


entry: 4.1.1.68
sysname: 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase
reaction: 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2 [RN:R04133]
iubmb_reaction: R04133
kegg_reaction: R04380
name:
--- 
- 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
- 5-carboxymethyl-2-oxo-hex-3-ene-1,6-dioate decarboxylase


entry: 4.1.1.70
sysname: 4-carboxybut-2-enoyl-CoA carboxy-lyase
reaction: 4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO2 [RN:R03028]
iubmb_reaction: R03028
name:
--- 
- glutaconyl-CoA decarboxylase
- glutaconyl coenzyme A decarboxylase
- pent-2-enoyl-CoA carboxy-lyase

comment:
The enzyme from Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.


entry: 4.1.1.71
sysname: 2-oxoglutarate carboxy-lyase
comment: Requires thiamine diphosphate. Highly specific.
reaction: 2-oxoglutarate = succinate semialdehyde + CO2 [RN:R00272]
iubmb_reaction: R00272
kegg_reaction: R00622
name:
--- 
- 2-oxoglutarate decarboxylase
- oxoglutarate decarboxylase
- alpha-ketoglutarate decarboxylase
- alpha-ketoglutaric decarboxylase
- pre-2-oxoglutarate decarboxylase


entry: 4.1.1.72
sysname: (3S)-3-methyl-2-oxopentanoate carboxy-lyase
reaction: (3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2 [RN:R03894]
iubmb_reaction: R03894
name:
--- 
- branched-chain-2-oxoacid decarboxylase
- branched-chain oxo acid decarboxylase
- branched-chain alpha-keto acid decarboxylase
- branched-chain keto acid decarboxylase
- BCKA

comment:
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.


entry: 4.1.1.76
sysname: 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropanoate-forming)
reaction: 2-aryl-2-methylmalonate = 2-arylpropanoate + CO2 [RN:R05173]
iubmb_reaction: R05173
name:
--- 
- arylmalonate decarboxylase
- AMDASE
- 2-aryl-2-methylmalonate carboxy-lyase
- 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropionate-forming)


entry: 4.1.1.78
sysname: acetylenedicarboxylate carboxy-lyase
reaction: acetylenedicarboxylate + H2O = pyruvate + CO2 [RN:R00218]
iubmb_reaction: R00218
kegg_reaction: R04177
name:
--- 
- acetylenedicarboxylate decarboxylase
- acetylenedicarboxylate hydratase
- acetylenedicarboxylate hydrase

comment:
The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate. It is thus analogous to EC 4.2.1.27 (acetylenecarboxylate hydratase) in its mechanism. Formerly EC 4.2.1.72


entry: 4.1.1.79
name: --- - sulfopyruvate decarboxylase
sysname: sulfopyruvate carboxy-lyase
reaction: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO2 [RN:R05774]
iubmb_reaction: R05774
comment:
Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.


entry: 4.1.1.81
name: --- - threonine-phosphate decarboxylase - L-threonine-O-3-phosphate decarboxylase - CobD
sysname: L-threonine-O-3-phosphate carboxy-lyase
reaction: L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2 [RN:R06530]
iubmb_reaction: R06530
comment:
A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.


entry: 4.1.1.82
name: --- - phosphonopyruvate decarboxylase
sysname: 3-phosphonopyruvate carboxy-lyase
reaction: 3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN:R04053]
iubmb_reaction: R04053
comment:
The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly.


entry: 4.1.1.83
name: --- - 4-hydroxyphenylacetate decarboxylase - p-hydroxyphenylacetate decarboxylase - p-Hpd - 4-Hpd
sysname: 4-hydroxyphenylacetate carboxy-lyase
reaction: (4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2 [RN:R07312]
iubmb_reaction: R07312
comment:
The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme.


entry: 4.1.1.84
sysname: D-dopachrome carboxy-lyase
reaction: D-dopachrome = 5,6-dihydroxyindole + CO2 [RN:R07313]
iubmb_reaction: R07313
name:
--- 
- D-dopachrome decarboxylase
- phenylpyruvate tautomerase II
- D-tautomerase
- D-dopachrome tautomerase

comment:
This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-alpha-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase)


entry: 4.1.1.85
sysname: 3-dehydro-L-gulonate-6-phosphate carboxy-lyase
reaction: 3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 [RN:R07125]
iubmb_reaction: R07125
name:
--- 
- 3-dehydro-L-gulonate-6-phosphate decarboxylase
- 3-keto-L-gulonate 6-phosphate decarboxylase
- UlaD
- SgaH
- SgbH
- KGPDC

comment:
Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.


entry: 4.1.1.86
name: --- - diaminobutyrate decarboxylase - DABA DC - L-2,4-diaminobutyrate decarboxylase
sysname: L-2,4-diaminobutanoate carboxy-lyase
reaction: L-2,4-diaminobutanoate = propane-1,3-diamine + CO2
comment:
A pyridoxal-phosphate protein that requires a divalent cation for activity [1]. 4-N-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate--2-oxoglutarate transaminase, which can supply the substrate for this enzyme.


entry: 4.1.1.-
name: --- []
reaction:
(1) Pyruvate + CO2 <=> 2-Hydroxyethylenedicarboxylate [RN:R00219]; (2) Homogentisate + Oxygen + NADPH <=> Gentisate aldehyde + CO2 + NADP+ + H+ + H2O [RN:R02518]; (3) 4-Coumarate <=> 4-Hydroxystyrene + CO2 [RN:R02952]; (4) 3-(4-Hydroxyphenyl)pyruvate <=> 4-Hydroxyphenylacetaldehyde + CO2 [RN:R03341]; (5) 3,4-Dihydroxy-trans-cinnamate <=> 3,4-Dihydroxystyrene + CO2 [RN:R03367]; (6) L-Dopachrome <=> 5,6-Dihydroxyindole + CO2 [RN:R03674]; (7) 4-Guanidinobutanal + CO2 <=> 2-Oxoarginine [RN:R04008]; (8) 3-Hydroxy-L-kynurenine <=> 3-Hydroxykynurenamine + CO2 [RN:R04172]; (9) (Z)-5-Oxohex-2-enedioate + H2O <=> 4-Hydroxy-2-oxopentanoate + CO2 [RN:R04223]; (10) (4R,5S)-4,5,6-Trihydroxy-2,3-dioxohexanoate + H2O <=> L-Xylonate + CO2 [RN:R04515]; (11) 3-Hexaprenyl-4,5-dihydroxybenzoate <=> 2-Hexaprenylphenol + CO2 [RN:R04712]; (12) 5-Aminoimidazole + CO2 <=> 5-Amino-4-imidazole carboxylate [RN:R04732]; (13) (4R,5S)-4,5,6-Trihydroxy-2,3-dioxohexanoate + H2O <=> L-Lyxonate + CO2 [RN:R04784]; (14) 5,6-Dihydroxyindole + CO2 <=> 2-Carboxy-2,3-dihydro-5,6-dihydroxyindole [RN:R04885]; (15) 3-Octaprenyl-4-hydroxybenzoate <=> 2-Octaprenylphenol + CO2 [RN:R04986]; (16) 4-Hydroxy-L-threonine <=> 3-Aminopropane-1,2-diol + CO2 [RN:R05087]; (17) Bis(4'-chlorophenyl)methane + CO2 <=> Bis(4'-chlorophenyl)acetate [RN:R05376]; (18) 2-Hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate <=> 2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate + CO2 [RN:R05377]; (19) 2-Hydroxyisophthalic acid <=> Salicylate + CO2 [RN:R06925]; (20) 3-Oxopropanoate <=> Acetaldehyde + CO2 [RN:R06973]


entry: 4.1.2.1
name: --- - Deleted entry
comment:
Deleted entry: hydroxyoxobutyrate aldolase. Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.2.1 created 1961, deleted 1972)


entry: 4.1.2.2
sysname: erythrulose-1-phosphate formaldehyde-lyase
reaction: erythrulose 1-phosphate = glycerone phosphate + formaldehyde [RN:R01014]
iubmb_reaction: R01014
name:
--- 
- ketotetrose-phosphate aldolase
- phosphoketotetrose aldolase
- erythrulose-1-phosphate synthetase
- erythrose-1-phosphate synthase


entry: 4.1.2.4
sysname: 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase
reaction: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde [RN:R01066]
iubmb_reaction: R01066
name:
--- 
- deoxyribose-phosphate aldolase
- phosphodeoxyriboaldolase
- deoxyriboaldolase
- deoxyribose-5-phosphate aldolase
- 2-deoxyribose-5-phosphate aldolase


entry: 4.1.2.6
name: --- - Deleted entry
comment:
Deleted entry: allothreonine aldolase. Reaction is due to EC 2.1.2.1 glycine hydroxymethyltransferase) (EC 4.1.2.6 created 1961, deleted 1972)


entry: 4.1.2.7
name: --- - Deleted entry
comment:
Deleted entry: ketose-1-phosphate aldolase. Now included with EC 4.1.2.13 fructose-bisphosphate aldolase (EC 4.1.2.7 created 1961, deleted 1972)


entry: 4.1.2.8
sysname: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase
reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
iubmb_reaction: (other) R02340
kegg_reaction: R02340
name:
--- 
- indole-3-glycerol-phosphate lyase
- tryptophan synthase alpha
- TSA
- indoleglycerolphosphate aldolase
- indole glycerol phosphate hydrolase
- indole synthase
- indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase
- indole-3-glycerol phosphate lyase
- IGL
- BX1

comment:
Forms part of the defence mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyses one of the steps in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) [1]. This enzyme resembles the alpha-subunit of EC 4.2.1.20, tryptophan synthase [3] but, unlike tryptophan synthase, its activity is independent of the beta-subunit and free indole is released [2].


entry: 4.1.2.9
name: --- - phosphoketolase
sysname: D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (phosphate-acetylating)
comment: A thiamine-diphosphate protein.
iubmb_reaction: R01621
kegg_reaction: R00761
reaction:
D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O [RN:R01621]


entry: 4.1.2.10
sysname: mandelonitrile benzaldehyde-lyase
reaction: mandelonitrile = cyanide + benzaldehyde [RN:R01767]
iubmb_reaction: R01767
kegg_reaction: R01409 R02811
name:
--- 
- mandelonitrile lyase
- hydroxynitrile lyase
- (R)-oxynitrilase
- oxynitrilase
- D-oxynitrilase
- D-alpha-hydroxynitrile lyase

comment:
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).


entry: 4.1.2.11
sysname: (S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase
reaction: (S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde [RN:R02676]
iubmb_reaction: R02676
kegg_reaction: R01409 R02811
name:
--- 
- hydroxymandelonitrile lyase
- hydroxynitrile lyase
- oxynitrilase
- Sorghum hydroxynitrile lyase

comment:
does not accept aliphatic hydroxynitriles, unlike EC 4.1.2.10 mandelonitrile lyase and EC 4.1.2.39 hydroxynitrilase.


entry: 4.1.2.13
sysname: D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
reaction: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate [RN:R01068]
iubmb_reaction: R01068 > R01070
kegg_reaction: R01829 R02568 R05378
name:
--- 
- fructose-bisphosphate aldolase
- aldolase
- fructose-1,6-bisphosphate triosephosphate-lyase
- fructose diphosphate aldolase
- diphosphofructose aldolase
- fructose 1,6-diphosphate aldolase
- ketose 1-phosphate aldolase
- phosphofructoaldolase
- zymohexase
- fructoaldolase
- fructose 1-phosphate aldolase
- fructose 1-monophosphate aldolase
- 1,6-Diphosphofructose aldolase
- SMALDO

comment:
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.


entry: 4.1.2.14
sysname: 2-dehydro-3-deoxy-D-gluconate-6-phosphate D-glyceraldehyde-3-phosphate-lyase
comment: Also acts on 2-oxobutanoate.
reaction: 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate [RN:R05605]
iubmb_reaction: R05605
kegg_reaction: R00471
name:
--- 
- 2-dehydro-3-deoxy-phosphogluconate aldolase
- phospho-2-keto-3-deoxygluconate aldolase
- KDPG aldolase
- phospho-2-keto-3-deoxygluconic aldolase
- 2-keto-3-deoxy-6-phosphogluconic aldolase
- 2-keto-3-deoxy-6-phosphogluconate aldolase
- 6-phospho-2-keto-3-deoxygluconate aldolase
- ODPG aldolase
- 2-oxo-3-deoxy-6-phosphogluconate aldolase
- 2-keto-3-deoxygluconate-6-P-aldolase
- 2-keto-3-deoxygluconate-6-phosphate aldolase


entry: 4.1.2.15
name: --- - Transferred to 2.5.1.54
comment:
Transferred entry: now EC 2.5.1.54, 3-deoxy-7-phosphoheptulonate synthase (EC 4.1.2.15 created 1965, modified 1976, deleted 2002)


entry: 4.1.2.16
name: --- - Transferred to 2.5.1.55
comment:
Transferred entry: now EC 2.5.1.55, 3-deoxy-8-phosphooctulonate synthase (EC 4.1.2.16 created 1965, deleted 2002)


entry: 4.1.2.18
sysname: 2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase
reaction: 2-dehydro-3-deoxy-L-pentonate = pyruvate + glycolaldehyde [RN:R01784]
iubmb_reaction: R01784
kegg_reaction: R03081
name:
--- 
- 2-dehydro-3-deoxy-L-pentonate aldolase
- 2-keto-3-deoxy-L-pentonate aldolase
- 2-keto-3-deoxy-L-arabonate aldolase
- 2-keto-3-deoxy-D-xylonate aldolase
- 3-deoxy-D-pentulosonic acid aldolase


entry: 4.1.2.19
sysname: L-rhamnulose-1-phosphate lactaldehyde-lyase
reaction: L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
iubmb_reaction: R02263
kegg_reaction: R01785
name:
--- 
- rhamnulose-1-phosphate aldolase
- rhamnulose phosphate aldolase
- L-rhamnulose 1-phosphate aldolase
- L-rhamnulose-phosphate aldolase


entry: 4.1.2.20
sysname: 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase
reaction: 2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde [RN:R03277]
iubmb_reaction: R03277
kegg_reaction: R02754
name:
--- 
- 2-dehydro-3-deoxyglucarate aldolase
- 2-keto-3-deoxyglucarate aldolase
- alpha-keto-beta-deoxy-D-glucarate aldolase


entry: 4.1.2.21
sysname: 2-dehydro-3-deoxy-D-galactonate-6-phosphate D-glyceraldehyde-3-phosphate-lyase
reaction: 2-dehydro-3-deoxy-D-galactonate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate [RN:R01064]
iubmb_reaction: R01064
name:
--- 
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- 6-phospho-2-keto-3-deoxygalactonate aldolase
- phospho-2-keto-3-deoxygalactonate aldolase
- 2-keto-3-deoxy-6-phosphogalactonic aldolase
- phospho-2-keto-3-deoxygalactonic aldolase
- 2-keto-3-deoxy-6-phosphogalactonic acid aldolase
- (KDPGal)aldolase


entry: 4.1.2.23
sysname: 3-deoxy-D-manno-octulosonate D-arabinose-lyase
reaction: 3-deoxy-D-manno-octulosonate = pyruvate + D-arabinose [RN:R01576]
iubmb_reaction: R01576
name:
--- 
- 3-deoxy-D-manno-octulosonate aldolase
- 2-keto-3-deoxyoctonate aldolase
- KDOaldolase
- 3-deoxyoctulosonic aldolase
- 2-keto-3-deoxyoctonic aldolase
- 3-deoxy-D-manno-octulosonic aldolase


entry: 4.1.2.25
name: --- - dihydroneopterin aldolase
sysname: 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropt eridine glycolaldehyde-lyase
iubmb_reaction: R03504
reaction:
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]


entry: 4.1.2.27
sysname: sphinganine-1-phosphate palmitaldehyde-lyase
comment: A pyridoxal-phosphate protein.
reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde [RN:R02464]
iubmb_reaction: R02464
kegg_reaction: R06516
name:
--- 
- sphinganine-1-phosphate aldolase
- dihydrosphingosine 1-phosphate aldolase
- sphinganine-1-phosphate alkanal-lyase
- sphinganine-1-phosphate lyase


entry: 4.1.2.28
sysname: 2-dehydro-3-deoxy-D-pentonate glycolaldehyde-lyase
reaction: 2-dehydro-3-deoxy-D-pentonate = pyruvate + glycolaldehyde [RN:R01782]
iubmb_reaction: R01782
name:
--- 
- 2-dehydro-3-deoxy-D-pentonate aldolase
- 2-keto-3-deoxy-D-pentonate aldolase
- 3-deoxy-D-pentulosonic acid aldolase


entry: 4.1.2.31
name: --- - Deleted entry
comment:
Deleted entry: 2-oxo-4-hydroxyglutarate aldolase. Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.2.31 created 1978, deleted 1982)


entry: 4.1.2.32
sysname: trimethylamine-N-oxide formaldehyde-lyase
reaction: trimethylamine N-oxide = dimethylamine + formaldehyde [RN:R02512]
iubmb_reaction: R02512
name:
--- 
- trimethylamine-oxide aldolase
- trimethylamine N-oxide formaldehyde-lyase
- trimethylamine N-oxide aldolase
- trimethylamine N-oxide demethylase


entry: 4.1.2.34
sysname: (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-carboxybenzaldehyde-lyase
reaction: (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate = 2-formylbenzoate + pyruvate
iubmb_reaction: (other) R03465
kegg_reaction: R03465
name:
--- 
- 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase
- 2'-carboxybenzalpyruvate aldolase
- (3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-carboxybenzaldehyde-lyase

comment:
Involved, with EC 1.13.11.38 (1-hydroxy-2-naphthoate 1,2-dioxygenase), in the metabolism of phenanthrene in bacteria.


entry: 4.1.2.37
sysname: acetone-cyanohydrin acetone-lyase
comment: Not identical with EC 4.1.2.10 (mandelonitrile lyase) or EC 4.1.2.11 (hydroxymandelonitrile lyase).
reaction: acetone cyanohydrin = cyanide + acetone [RN:R01553]
iubmb_reaction: R01553
name:
--- 
- acetone-cyanohydrin lyase
- alpha-hydroxynitrile lyase
- hydroxynitrile lyase
- acetone-cyanhydrin lyase [mis-spelt]


entry: 4.1.2.39
name: --- - hydroxynitrilase - hydroxynitrile lyase - oxynitrilase
sysname: 2-hydroxyisobutyronitrile acetone-lyase
reaction: 2-hydroxyisobutyronitrile = cyanide + acetone [RN:R01553]
iubmb_reaction: R01553
comment:
the enzyme from Hevea (rubber tree) and Manihot spp. (cassava) accepts aliphatic and aromatic hydroxynitriles, unlike EC 4.1.2.11 (hydroxymandelonitrile lyase) which does not act on aliphatic hydroxynitriles. 2-Hydroxyisobutyronitrile (acetone cyanohydrin) is liberated by glycosidase action on linamarin.


entry: 4.1.2.40
name: --- - tagatose-bisphosphate aldolase
sysname: D-tagatose-1,6-bisphosphate triosephosphate lyase
reaction: D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate [RN:R01069]
iubmb_reaction: R01069
comment:
enzyme activity is stimulated by certain divalent cations. It is involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.


entry: 4.1.2.41
name: --- - vanillin synthase
sysname: 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA:vanillin lyase (acetyl-CoA-forming)
reaction: 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA = vanillin + acetyl-CoA [RN:R05773]
iubmb_reaction: R05773
comment:
Involved, together with EC 4.2.1.101 trans-feruloyl-CoA hydratase, in the production of vanillin from trans-ferulic acid. Vanillin is converted to vanillate by EC 1.2.1.67 vanillin dehydrogenase.


entry: 4.1.2.-
name: --- []
reaction:
(1) Acetaldehyde + Pyruvate <=> 4-Hydroxy-2-oxopentanoate [RN:R00750]; (2) 4-Hydroxy-2-oxo-heptanedioate <=> Succinate semialdehyde + Pyruvate [RN:R01645]; (3) Succinate semialdehyde + Pyruvate <=> 2,4-Dihydroxyhept-2-enedioate [RN:R01647]; (4) 2-Dehydro-3-deoxy-L-rhamnonate <=> (S)-Lactaldehyde + Pyruvate [RN:R02261]; (5) 4-Trimethylammoniobutanal + Glycine <=> 3-Hydroxy-N6,N6,N6-trimethyl-L-lysine [RN:R03284]; (6) Hexadecenal + Ethanolamine phosphate <=> Sphingosine 1-phosphate [RN:R05104]; (7) D-Ribulose 5-phosphate + Formaldehyde <=> D-arabino-3-Hexulose 6-phosphate [RN:R05338]; (8) cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate + H2O <=> 1-Hydroxy-2-naphthaldehyde + Pyruvate [RN:R05648]


entry: 4.1.3.1
sysname: isocitrate glyoxylate-lyase
comment: The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
reaction: isocitrate = succinate + glyoxylate [RN:R00479]
iubmb_reaction: R00479
name:
--- 
- isocitrate lyase
- isocitrase
- isocitritase
- isocitratase
- threo-D(s)-isocitrate glyoxylate-lyase


entry: 4.1.3.3
sysname: N-acetylneuraminate pyruvate-lyase
reaction: N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate [RN:R01811]
iubmb_reaction: R01811
name:
--- 
- N-acetylneuraminate lyase
- N-acetylneuraminic acid aldolase
- acetylneuraminate lyase
- sialic aldolase
- sialic acid aldolase
- sialate lyase
- N-acetylneuraminic aldolase
- neuraminic aldolase
- N-acetylneuraminate aldolase
- neuraminic acid aldolase
- neuraminate aldolase
- N-acetylneuraminic lyase
- N-acetylneuraminic acid lyase
- NPL
- NALase
- NANA lyase
- acetylneuraminate pyruvate-lyase

comment:
Also acts on N-glycoloylneuraminate, and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.


entry: 4.1.3.4
sysname: (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase
reaction: (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate [RN:R01360]
iubmb_reaction: R01360
name:
--- 
- hydroxymethylglutaryl-CoA lyase
- hydroxymethylglutaryl coenzyme A-cleaving enzyme
- hydroxymethylglutaryl coenzyme A lyase
- 3-hydroxy-3-methylglutaryl coenzyme A lyase
- 3-hydroxy-3-methylglutaryl CoA cleaving enzyme
- 3-hydroxy-3-methylglutaryl-CoA lyase


entry: 4.1.3.5
name: --- - Transferred to 2.3.3.10
comment:
Transferred entry: now EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5 created 1961, deleted 2002)


entry: 4.1.3.6
sysname: citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetate]
reaction: citrate = acetate + oxaloacetate [RN:R00362]
iubmb_reaction: R00362
name:
--- 
- citrate (pro-3S)-lyase
- citrase
- citratase
- citritase
- citridesmolase
- citrate aldolase
- citric aldolase
- citrate lyase
- citrate oxaloacetate-lyase

comment:
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.10 (citrate CoA-transferase) and EC 4.1.3.34 (citryl-CoA lyase). EC 3.1.2.16 (citrate lyase deacetylase), deacetylates and inactivates the enzyme.


entry: 4.1.3.8
name: --- - Transferred to 2.3.3.8
comment:
Transferred entry: now EC 2.3.3.8, ATP citrate synthase (EC 4.1.3.8 created 1965, modified 1986, deleted 2002)


entry: 4.1.3.9
name: --- - Transferred to 2.3.3.11
comment:
Transferred entry: now EC 2.3.3.11, 2-hydroxyglutarate synthase (EC 4.1.3.9 created 1965, deleted 2002)


entry: 4.1.3.10
name: --- - Transferred to 2.3.3.7
comment:
Transferred entry: now EC 2.3.3.7, 3-ethylmalate synthase (EC 4.1.3.10 created 1965, modified 1983, deleted 2002)


entry: 4.1.3.11
name: --- - Transferred to 2.3.3.12
comment:
Transferred entry: now EC 2.3.3.12, 3-propylmalate synthase (EC 4.1.3.11 created 1972, deleted 2002)


entry: 4.1.3.12
name: --- - Transferred to 2.3.3.13
comment:
Transferred entry: now EC 2.3.3.13, 2-isopropylmalate synthase (EC 4.1.3.12 created 1972, deleted 2002)


entry: 4.1.3.14
sysname: erythro-3-hydroxy-L(s)-aspartate glyoxylate-lyase
reaction: erythro-3-hydroxy-L(s)-aspartate = glycine + glyoxylate [RN:R00478]
iubmb_reaction: R00478
name:
--- 
- 3-hydroxyaspartate aldolase
- erythro-beta-hydroxyaspartate aldolase
- erythro-beta-hydroxyaspartate glycine-lyase


entry: 4.1.3.15
name: --- - Transferred to 2.2.1.5
comment:
Transferred entry: now EC 2.2.1.5, 2-hydroxy-3-oxoadipate synthase (EC 4.1.3.15 created 1972, deleted 2002)


entry: 4.1.3.16
sysname: 4-hydroxy-2-oxoglutarate glyoxylate-lyase
comment: Acts on both stereoisomers. Previously listed also as EC 4.1.2.31.
reaction: 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate [RN:R00470]
iubmb_reaction: R00470 > R00471
name:
--- 
- 4-hydroxy-2-oxoglutarate aldolase
- 2-oxo-4-hydroxyglutarate aldolase
- hydroxyketoglutaric aldolase
- 4-hydroxy-2-ketoglutaric aldolase
- 2-keto-4-hydroxyglutaric aldolase
- 4-hydroxy-2-ketoglutarate aldolase
- 2-keto-4-hydroxyglutarate aldolase
- 2-oxo-4-hydroxyglutaric aldolase
- DL-4-hydroxy-2-ketoglutarate aldolase
- hydroxyketoglutarate aldolase
- 2-keto-4-hydroxybutyrate aldolase


entry: 4.1.3.17
sysname: 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase
comment: Also acts on 4-hydroxy-4-methyl-2-oxoadipate and 4-carboxy-4-hydroxy-2-oxohexadioate.
reaction: 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
iubmb_reaction: (other) R00007 R00008 R00350
kegg_reaction: R00007 R00008 R00350
name:
--- 
- 4-hydroxy-4-methyl-2-oxoglutarate aldolase
- pyruvate aldolase
- gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase
- 4-hydroxy-4-methyl-2-ketoglutarate aldolase


entry: 4.1.3.19
name: --- - Transferred to 2.5.1.56
comment:
Transferred entry: now EC 2.5.1.56, N-acetylneuraminate synthase (EC 4.1.2.19 created 1972, deleted 2002)


entry: 4.1.3.20
name: --- - Transferred to 2.5.1.57
comment:
Transferred entry: now EC 2.5.1.57, N-acylneuraminate-9-phosphate synthase (EC 4.1.3.20 created 1972, deleted 2002)


entry: 4.1.3.22
sysname: (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase
reaction: (2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate [RN:R00325]
iubmb_reaction: R00325
kegg_reaction: R00237 R03153
name:
--- 
- citramalate lyase
- citramalate pyruvate-lyase
- citramalate synthase
- citramalic-condensing enzyme
- citramalate synthetase
- citramalic synthase
- (S)-citramalate lyase
- (+)-citramalate pyruvate-lyase
- citramalate pyruvate lyase
- (3S)-citramalate pyruvate-lyase

comment:
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC 4.1.3.25 (citramalyl-CoA lyase).


entry: 4.1.3.25
name: --- - citramalyl-CoA lyase - citramalyl coenzyme A lyase - (+)-CMA-CoA lyase
sysname: (3S)-citramalyl-CoA pyruvate-lyase
reaction: (3S)-citramalyl-CoA = acetyl-CoA + pyruvate [RN:R00237]
iubmb_reaction: R00237
comment:
The enzyme is a component of EC 4.1.3.22 citramalate lyase. Also acts on (3S)-citramalyl thioacyl-carrier protein.


entry: 4.1.3.26
sysname: 3-hydroxy-3-isohexenylglutaryl-CoA isopentenylacetoacetyl-CoA-lyase
comment: Also acts on the hydroxy derivative of farnesoyl-CoA.
iubmb_reaction: R04287
name:
--- 
- 3-hydroxy-3-isohexenylglutaryl-CoA lyase
- beta-hydroxy-beta-isohexenylglutaryl CoA-lyase
- hydroxyisohexenylglutaryl-CoA:acetatelyase
- 3-hydroxy-3-isohexenylglutaryl coenzyme A lyase

reaction:
3-hydroxy-3-(4-methylpent-3-en-1-yl)-glutaryl-CoA = 7-methyl-3-oxooctanoyl-CoA + acetate [RN:R04287]


entry: 4.1.3.27
name: --- - anthranilate synthase - anthranilate synthetase - chorismate lyase
sysname: chorismate pyruvate-lyase (amino-accepting)
reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate [RN:R00986]
iubmb_reaction: R00986
kegg_reaction: R00985
comment:
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.


entry: 4.1.3.29
name: --- - Transferred to 2.3.3.4
comment:
Transferred entry: now EC 2.3.3.4, decylhomocitrate synthase (EC 4.1.3.29 created 1976, deleted 2002)


entry: 4.1.3.30
name: --- - methylisocitrate lyase - 2-methylisocitrate lyase - MICL
sysname: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase
reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate [RN:R00409]
iubmb_reaction: R00409
comment:
The enzyme acts on threo-D(s)-2-methylisocitrate, but not on threo-D(s)-isocitrate, threo-DL-isocitrate or erythro-L(s)-isocitrate.


entry: 4.1.3.31
name: --- - Transferred to 2.3.3.5
comment:
Transferred entry: now EC 2.3.3.5, 2-methylcitrate synthase (EC 4.1.3.31 created 1978, deleted 2002)


entry: 4.1.3.34
name: --- - citryl-CoA lyase
sysname: (3S)-citryl-CoA oxaloacetate-lyase
reaction: (3S)-citryl-CoA = acetyl-CoA + oxaloacetate [RN:R00354]
iubmb_reaction: R00354
comment:
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein.


entry: 4.1.3.37
name: --- - Transferred to 2.2.1.7
comment:
Transferred entry: now EC 2.2.1.7, 1-deoxy-D-xylulose 5-phosphate synthase (EC 4.1.3.37 created 2001, deleted 2002)


entry: 4.1.3.38
name: --- - aminodeoxychorismate lyase - enzyme X - 4-amino-4-deoxychorismate lyase
sysname: 4-amino-4-deoxychorismate pyruvate-lyase
reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate [RN:R05553]
iubmb_reaction: R05553
comment:
A pyridoxal-phosphate protein. Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 6.3.5.8, aminodeoxychorismate synthase, to form p-aminobenzoate.


entry: 4.1.3.39
name: --- - 4-hydroxy-2-oxovalerate aldolase - 4-hydroxy-2-ketovalerate aldolase - HOA - DmpG
sysname: 4-hydroxy-2-oxovalerate pyruvate-lyase
reaction: 4-hydroxy-2-oxovalerate = pyruvate + acetaldehyde
comment:
Requires Mn2+ for maximal activity [1]. The enzyme from Pseudomonas putida is also stimulated by the presence of NADH [1]. In Pseudomonas species, this enzyme forms part of a bifunctional enzyme with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). It catalyses the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol [1].


entry: 4.1.3.-
name: --- []
reaction:
(1) Acetaldehyde + Pyruvate <=> 4-Hydroxy-2-oxopentanoate [RN:R00750]; (2) 4-Hydroxybenzoate + Pyruvate <=> Chorismate [RN:R01302]; (3) Succinate semialdehyde-thiamin diphosphate anion + Isochorismate <=> 2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate + Thiamin diphosphate + Pyruvate [RN:R04992]; (4) 2-Propylmalate + CoA <=> 2-Oxopentanoic acid + Acetyl-CoA [RN:R05063]; (5) Propanal + Pyruvate <=> 4-Hydroxy-2-oxohexanoic acid [RN:R05298]


entry: 4.1.99.1
name: --- - tryptophanase - L-tryptophanase
sysname: L-tryptophan indole-lyase (deaminating)
reaction: L-tryptophan + H2O = indole + pyruvate + NH3 [RN:R00673]
iubmb_reaction: R00673
comment:
A pyridoxal-phosphate protein, requiring K+. Also catalyses 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.


entry: 4.1.99.2
name: --- - tyrosine phenol-lyase - beta-tyrosinase
sysname: L-tyrosine phenol-lyase (deaminating)
reaction: L-tyrosine + H2O = phenol + pyruvate + NH3 [RN:R00728]
iubmb_reaction: R00728
comment:
A pyridoxal-phosphate protein. The enzyme also slowly catalyses pyruvate formation from D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.


entry: 4.1.99.3
sysname: deoxyribocyclobutadipyrimidine pyrimidine-lyase
reaction: cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
iubmb_reaction: (other) R00034
kegg_reaction: R00034
name:
--- 
- deoxyribodipyrimidine photo-lyase
- photoreactivating enzyme
- DNA photolyase
- DNA-photoreactivating enzyme
- DNA cyclobutane dipyrimidine photolyase
- deoxyribonucleic photolyase
- deoxyribodipyrimidine photolyase
- photolyase
- PRE
- PhrB photolyase
- deoxyribonucleic cyclobutane dipyrimidine photolyase
- phr A photolyase
- dipyrimidine photolyase (photosensitive)
- deoxyribonucleate pyrimidine dimer lyase (photosensitive)

comment:
A flavoprotein (FAD), containing a second chromophore group. The enzyme catalyses the reactivation by light of irradiated DNA. A similar reactivation of irradiated RNA is probably due to a separate enzyme.


entry: 4.1.99.4
name: --- - Transferred to 3.5.99.7
comment:
Transferred entry: now EC 3.5.99.7, 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4 created 1981, deleted 2002)


entry: 4.1.99.5
name: --- - octadecanal decarbonylase - decarbonylase - aldehyde decarbonylase
sysname: octadecanal alkane-lyase
reaction: octadecanal = heptadecane + CO [RN:R03728]
iubmb_reaction: R03728
comment:
Involved in the biosynthesis of alkanes in the pea Pisum sativum from fatty acids of chain length C18 to C32. Inhibited by metal-chelating agents.


entry: 4.1.99.7
name: --- - Transferred to 4.2.3.9
comment:
Transferred entry: now EC 4.2.3.9, aristolochene synthase (EC 4.1.99.7 created 1992 as EC 2.5.1.40, transferred 1999 to EC 4.1.99.7, deleted 2000)


entry: 4.1.99.11
name: --- - benzylsuccinate synthase
sysname: benzylsuccinate fumarate-lyase
reaction: toluene + fumarate = benzylsuccinate [RN:R05598]
iubmb_reaction: R05598
comment:
A glycyl radical enzyme that is inhibited by benzyl alcohol, benzaldehyde, phenylhydrazine and is inactivated by oxygen.


entry: 4.1.99.-
name: --- []
reaction:
(1) 3-Oxo-4-methylpentanoic acid <=> (R)-3-Methyl-2-oxobutanoate + Acetate [RN:R05067]; (2) Isochorismate <=> Salicylate + Pyruvate [RN:R06602]; (3) 2-Methylnaphthalene + Fumarate <=> Naphthyl-2-methyl-succinic acid [RN:R06903]


entry: 4.2.1.1
sysname: carbonate hydro-lyase
comment: A zinc protein.
reaction: H2CO3 = CO2 + H2O [RN:R00132]
iubmb_reaction: R00132
name:
--- 
- carbonate dehydratase
- carbonic anhydrase
- anhydrase
- carbonate anhydrase
- carbonic acid anhydrase
- carboxyanhydrase
- carbonic anhydrase A


entry: 4.2.1.3
name: --- - aconitate hydratase - cis-aconitase - aconitase
sysname: citrate(isocitrate) hydro-lyase
iubmb_reaction: R01325 R01900
kegg_reaction: R01324
comment:
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.

reaction:
(1) citrate =isocitrate [RN:R01325]; (2) (1a) citrate = cis-aconitate + H2O [RN:R01900]; (3) (1b) cis-aconitate + H2O = isocitrate


entry: 4.2.1.4
name: --- - citrate dehydratase
sysname: citrate hydro-lyase
reaction: citrate = cis-aconitate + H2O [RN:R01325]
iubmb_reaction: R01325
comment:
cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. Does not act on isocitrate.


entry: 4.2.1.8
sysname: D-mannonate hydro-lyase
reaction: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O [RN:R05606]
iubmb_reaction: R05606
name:
--- 
- mannonate dehydratase
- mannonic hydrolase
- mannonate hydrolyase
- altronic hydro-lyase
- altronate hydrolase
- D-mannonate hydrolyase


entry: 4.2.1.9
sysname: 2,3-dihydroxy-acid hydro-lyase
reaction: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O [RN:R01209]
iubmb_reaction: R01209 > R04441
kegg_reaction: R05070
name:
--- 
- dihydroxy-acid dehydratase
- acetohydroxyacid dehydratase
- alpha,beta-dihydroxyacid dehydratase
- 2,3-dihydroxyisovalerate dehydratase
- alpha,beta-dihydroxyisovalerate dehydratase
- dihydroxy acid dehydrase
- DHAD


entry: 4.2.1.10
sysname: 3-dehydroquinate hydro-lyase
reaction: 3-dehydroquinate = 3-dehydroshikimate + H2O [RN:R03084]
iubmb_reaction: R03084
name:
--- 
- 3-dehydroquinate dehydratase
- 3-dehydroquinate hydrolase
- DHQase
- dehydroquinate dehydratase
- 3-dehydroquinase
- 5-dehydroquinase
- dehydroquinase
- 5-dehydroquinate dehydratase
- 5-dehydroquinate hydro-lyase


entry: 4.2.1.11
sysname: 2-phospho-D-glycerate hydro-lyase
comment: Also acts on 3-phospho-D-erythronate.
reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O [RN:R00658]
iubmb_reaction: R00658
kegg_reaction: R04206
name:
--- 
- phosphopyruvate hydratase
- enolase
- 2-phosphoglycerate dehydratase
- 14-3-2-protein
- nervous-system specific enolase
- phosphoenolpyruvate hydratase
- 2-phosphoglyceric dehydratase
- 2-phosphoglycerate enolase
- gamma-enolase


entry: 4.2.1.12
sysname: 6-phospho-D-gluconate hydro-lyase
reaction: 6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O [RN:R02036]
iubmb_reaction: R02036
name:
--- 
- phosphogluconate dehydratase
- 6-phosphogluconate dehydratase
- 6-phosphogluconic dehydrase
- gluconate-6-phosphate dehydratase
- gluconate 6-phosphate dehydratase
- 6-phosphogluconate dehydrase


entry: 4.2.1.15
name: --- - Deleted entry
comment:
Deleted entry: homoserine dehydratase. Identical with EC 4.4.1.1 cystathionine gamma-lyase (EC 4.2.1.15 created 1961, deleted 1972)


entry: 4.2.1.16
name: --- - Transferred to 4.3.1.19
comment:
Transferred entry: now EC 4.3.1.19, threonine ammonia-lyase (EC 4.2.1.16 created 1961, deleted 2001)


entry: 4.2.1.17
sysname: (3S)-3-hydroxyacyl-CoA hydro-lyase
reaction: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685 R07314]
iubmb_reaction: R02685 > R03026 R03045 R04170 R04204 R04224 R04738 R04740 R04744 R04746 R04749; R07314
kegg_reaction: R03224 R04137 R05595 R06411 R06412 R06942
name:
--- 
- enoyl-CoA hydratase
- enoyl hydrase
- unsaturated acyl-CoA hydratase
- beta-hydroxyacyl-CoA dehydrase
- beta-hydroxyacid dehydrase
- hydratase, enoyl coenzyme A
- acyl coenzyme A hydrase
- crotonase
- crotonyl hydrase
- 2-octenoyl coenzyme A hydrase
- enoyl coenzyme A hydratase
- 2-enoyl-CoA hydratase
- short-chain enoyl-CoA hydratase
- ECH
- trans-2-enoyl-CoA hydratase
- enoyl coenzyme A hydrase (D)
- enoyl coenzyme A hydrase (L)
- short chain enoyl coenzyme A hydratase
- D-3-hydroxyacyl-CoA dehydratase
- enol-CoA hydratase

comment:
Acts in the reverse direction. With cis-compounds, yields (3R)-3-hydroxyacyl-CoA. cf. EC 4.2.1.74 long-chain-enoyl-CoA hydratase.


entry: 4.2.1.18
sysname: (S)-3-hydroxy-3-methylglutaryl-CoA hydro-lyase
reaction: (S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H2O [RN:R02085]
iubmb_reaction: R02085
name:
--- 
- methylglutaconyl-CoA hydratase
- methylglutaconyl coenzyme A hydratase
- 3-methylglutaconyl CoA hydratase
- methylglutaconase


entry: 4.2.1.19
name: --- - imidazoleglycerol-phosphate dehydratase - IGP dehydratase
sysname: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate hydro-lyase
iubmb_reaction: R03457
reaction:
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O [RN:R03457]


entry: 4.2.1.20
sysname: L-serine hydro-lyase (adding indoleglycerol-phosphate)
iubmb_reaction: R02722
kegg_reaction: R00674 R02340
name:
--- 
- tryptophan synthase
- L-tryptophan synthetase
- indoleglycerol phosphate aldolase
- tryptophan desmolase
- tryptophan synthetase

comment:
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and glyceraldehyde 3-phosphate. The indole then migrates to the beta-subunit where, with serine in the presence of pyridoxal 5'-phosphate, it is converted to tryptophan. Also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.1.2.8). In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].

reaction:
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate [RN:R02722]


entry: 4.2.1.21
name: --- - Deleted entry
comment:
Deleted entry: cystathionine beta-synthase. Now EC 4.2.1.22 cystathionine beta-synthase (EC 4.2.1.21 created 1961, deleted 1964)


entry: 4.2.1.22
sysname: L-serine hydro-lyase (adding homocysteine)
reaction: L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
iubmb_reaction: R01290
kegg_reaction: R00891 R01289 R04942
name:
--- 
- cystathionine beta-synthase
- serine sulfhydrase
- beta-thionase
- methylcysteine synthase
- cysteine synthase
- serine sulfhydrylase

comment:
A pyridoxal-phosphate protein. A multifunctional enzyme: catalyses beta-replacement reactions between L-serine, L-cysteine, cysteine thioethers, or some other beta-substituted alpha-L-amino acids, and a variety of mercaptans.


entry: 4.2.1.23
name: --- - Deleted entry
comment:
Deleted entry: methylcysteine synthase. The reaction was due to a side-reaction of EC 4.2.1.22 cystathionine beta-synthase (EC 4.2.1.23 created 1961, deleted 1972)


entry: 4.2.1.24
sysname: 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing)
comment: The fungal enzyme is a metalloprotein.
reaction: 2 5-aminolevulinate = porphobilinogen + 2 H2O [RN:R00036]
iubmb_reaction: R00036
name:
--- 
- porphobilinogen synthase
- aminolevulinate dehydratase
- delta-aminolevulinate dehydratase
- delta-aminolevulinic acid dehydrase
- delta-aminolevulinic acid dehydratase
- aminolevulinic dehydratase
- delta-aminolevulinic dehydratase
- 5-levulinic acid dehydratase


entry: 4.2.1.26
name: --- - Transferred to 4.3.1.9
comment:
Transferred entry: now EC 4.3.1.9, aminodeoxygluconate ammonia-lyase (EC 4.2.1.26 created 1965, deleted 2002)


entry: 4.2.1.27
sysname: 3-oxopropanoate hydro-lyase
reaction: 3-oxopropanoate = propynoate + H2O [RN:R01611]
iubmb_reaction: R01611
kegg_reaction: R01367
name:
--- 
- acetylenecarboxylate hydratase
- acetylenemonocarboxylate hydratase
- alkynoate hydratase
- acetylenemonocarboxylate hydrase
- acetylenemonocarboxylic acid hydrase
- malonate-semialdehyde dehydratase

comment:
The reaction is effectively irreversible, favouring oxopropanoate (malonic semialdehyde) and its tautomers. Also acts on but-3-ynoate forming acetoacetate. The mechanism appears to involve hydration of the acetylene to 3-hydroxypropenoate, which will spontaneously tautomerize to 3-oxopropanoate. It is thus analogous to EC 4.1.1.78, acetylenedicarboxylate decarboxylase, in its mechanism.


entry: 4.2.1.28
sysname: propane-1,2-diol hydro-lyase
comment: Requires a cobamide coenzyme. Also dehydrates ethylene glycol to acetaldehyde.
reaction: propane-1,2-diol = propanal + H2O [RN:R02376]
iubmb_reaction: R02376
name:
--- 
- propanediol dehydratase
- meso-2,3-butanediol dehydrase
- diol dehydratase
- DL-1,2-propanediol hydro-lyase
- diol dehydrase
- adenosylcobalamin-dependent diol dehydratase
- propanediol dehydrase
- coenzyme B12-dependent diol dehydrase
- 1,2-propanediol dehydratase
- dioldehydratase


entry: 4.2.1.29
name: --- - Transferred to 4.99.1.6
comment:
Transferred entry: now EC 4.99.1.6, indoleacetaldoxime dehydratase. The enzyme was classified incorrectly as a C-O lyase when the bond broken is a N-O bond. (EC 4.2.1.29 created 1965, deleted 2004)


entry: 4.2.1.32
sysname: (R,R)-tartrate hydro-lyase
reaction: (R,R)-tartrate = oxaloacetate + H2O [RN:R00339]
iubmb_reaction: R00339
name:
--- 
- L(+)-tartrate dehydratase
- tartrate dehydratase
- tartaric acid dehydrase
- L-tartrate dehydratase
- L-(+)-tartaric acid dehydratase

comment:
The enzyme exists in an inactive low-molecular-mass form, which is converted into active enzyme in the presence of Fe2+ and thiol. cf. EC 4.2.1.81 D(-)-tartrate dehydratase.


entry: 4.2.1.33
sysname: (2R,3S)-3-isopropylmalate hydro-lyase
reaction: (2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H2O [RN:R04001]
iubmb_reaction: R04001
kegg_reaction: R03968
name:
--- 
- 3-isopropylmalate dehydratase
- beta-isopropylmalate dehydratase
- isopropylmalate isomerase
- alpha-isopropylmalate isomerase

comment:
The enzyme also hydrates the product to (2S)-2-isopropylmalate, thus bringing about an interconversion between the two isomers.


entry: 4.2.1.34
sysname: (S)-2-methylmalate hydro-lyase
comment: Also hydrates fumarate to (S)-malate.
reaction: (S)-2-methylmalate = 2-methylfumarate + H2O [RN:R03693]
iubmb_reaction: R03693
name:
--- 
- (S)-2-methylmalate dehydratase
- mesaconate hydratase
- (+)-citramalate hydro-lyase
- L-citramalate hydrolase
- citramalate dehydratase
- (+)-citramalic hydro-lyase
- mesaconate mesaconase
- mesaconase


entry: 4.2.1.35
sysname: (R)-2-methylmalate hydro-lyase
comment: Requires Fe2+.
reaction: (R)-2-methylmalate = 2-methylmaleate + H2O [RN:R03896]
iubmb_reaction: R03896
name:
--- 
- (R)-2-methylmalate dehydratase
- citraconate hydratase
- citraconase
- citramalate hydro-lyase
- (-)-citramalate hydro-lyase


entry: 4.2.1.37
name: --- - Transferred to 3.3.2.4
comment:
Transferred entry: now EC 3.3.2.4 trans-epoxysuccinate hydrolase (EC 4.2.1.37 created 1972, deleted 1992)


entry: 4.2.1.38
name: --- - Transferred to 4.3.1.20
comment:
Transferred entry: now EC 4.3.1.20, erythro-3-hydroxyaspartate ammonia-lyase (EC 4.2.1.38 created 1972, deleted 2001)


entry: 4.2.1.41
sysname: 5-dehydro-4-deoxy-D-glucarate hydro-lyase (decarboxylating)
reaction: 5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + H2O + CO2 [RN:R02279]
iubmb_reaction: R02279
name:
--- 
- 5-dehydro-4-deoxyglucarate dehydratase
- 5-keto-4-deoxy-glucarate dehydratase
- deoxyketoglucarate dehydratase
- D-4-deoxy-5-ketoglucarate hydro-lyase


entry: 4.2.1.46
sysname: dTDP-glucose 4,6-hydro-lyase
comment: Requires bound NAD+.
reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O [RN:R06513]
iubmb_reaction: R06513 > R02771
name:
--- 
- dTDP-glucose 4,6-dehydratase
- thymidine diphosphoglucose oxidoreductase
- TDP-glucose oxidoreductase


entry: 4.2.1.47
sysname: GDP-mannose 4,6-hydro-lyase
reaction: GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O [RN:R00888]
iubmb_reaction: R00888
name:
--- 
- GDP-mannose 4,6-dehydratase
- guanosine 5'-diphosphate-D-mannose oxidoreductase
- guanosine diphosphomannose oxidoreductase
- guanosine diphosphomannose 4,6-dehydratase
- GDP-D-mannose dehydratase
- GDP-D-mannose 4,6-dehydratase
- Gmd

comment:
The bacterial enzyme requires bound NAD+. This enzyme forms the first step in the biosynthesis of GDP-D-rhamnose and GDP-L-fucose. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalysing the above reaction as well as the reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase [5]. Belongs to the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr and Ser/Thr residues [6].


entry: 4.2.1.51
name: --- - prephenate dehydratase
sysname: prephenate hydro-lyase (decarboxylating)
reaction: prephenate = phenylpyruvate + H2O + CO2 [RN:R01373]
iubmb_reaction: R01373
kegg_reaction: R00691
comment:
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.


entry: 4.2.1.52
sysname: L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing)
iubmb_reaction: R02292
name:
--- 
- dihydrodipicolinate synthase
- dihydropicolinate synthetase
- dihydrodipicolinic acid synthase

reaction:
L-aspartate 4-semialdehyde + pyruvate = (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O [RN:R02292]


entry: 4.2.1.54
sysname: lactoyl-CoA hydro-lyase
reaction: lactoyl-CoA = acryloyl-CoA + H2O [RN:R02963]
iubmb_reaction: R02963
name:
--- 
- lactoyl-CoA dehydratase
- lactoyl coenzyme A dehydratase
- lactyl-coenzyme A dehydrase
- lactyl CoA dehydratase
- acrylyl coenzyme A hydratase


entry: 4.2.1.55
sysname: (3R)-3-hydroxybutanoyl-CoA hydro-lyase
comment: Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein.
reaction: (3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O [RN:R03027]
iubmb_reaction: R03027
name:
--- 
- 3-hydroxybutyryl-CoA dehydratase
- D-3-hydroxybutyryl coenzyme A dehydratase
- D-3-hydroxybutyryl-CoA dehydratase
- enoyl coenzyme A hydrase (D)


entry: 4.2.1.57
sysname: 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase
comment: Also acts on dimethylacryloyl-CoA and farnesoyl-CoA.
iubmb_reaction: R03493
name:
--- 
- isohexenylglutaconyl-CoA hydratase
- 3-hydroxy-3-isohexenylglutaryl-CoA-hydrolase
- isohexenylglutaconyl coenzyme A hydratase
- beta-isohexenylglutaconyl-CoA-hydratase

reaction:
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 3-(4-methylpent-3-en-1-yl)-pent-2-enedioyl-CoA + H2O [RN:R03493]


entry: 4.2.1.58
sysname: (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase
comment: Is specific for short chain-length 3-hydroxyacyl-[acyl-carrier protein] derivatives (C4 to C8).
iubmb_reaction: R04428
kegg_reaction: R04535 R04537 R04954 R04965
name:
--- 
- crotonoyl-[acyl-carrier-protein] hydratase
- beta-hydroxybutyryl acyl carrier protein dehydrase
- beta-hydroxybutyryl acyl carrier protein (ACP) dehydrase
- enoyl acyl carrier protein hydrase
- crotonyl acyl carrier protein hydratase
- 3-hydroxybutyryl acyl carrier protein dehydratase

reaction:
(3R)-3-hydroxybutanoyl-[acyl-carrier protein] = but-2-enoyl-[acyl-carrier protein] + H2O [RN:R04428]


entry: 4.2.1.59
sysname: (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase
comment: Is specific for 3-hydroxyacyl-[acyl-carrier protein] derivatives (C6 to C12).
reaction: (3R)-3-hydroxyoctanoyl-[acyl-carrier protein] = 2-octenoyl-[acyl-carrier protein] + H2O [RN:R04537]
iubmb_reaction: R04537
name:
--- 
- 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase
- D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase
- D-3-hydroxyoctanoyl-acyl carrier protein dehydratase
- beta-hydroxyoctanoyl-acyl carrier protein dehydrase
- beta-hydroxyoctanoyl thioester dehydratase
- beta-hydroxyoctanoyl-ACP-dehydrase


entry: 4.2.1.60
sysname: (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase
comment: Specific for C10 chain length.
iubmb_reaction: R04414 > R04535; R04416
kegg_reaction: R04965
name:
--- 
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase
- 3-hydroxydecanoyl-acyl carrier protein dehydrase
- 3-hydroxydecanoyl-acyl carrier protein dehydratase
- beta-hydroxydecanoyl thioester dehydrase
- beta-hydroxydecanoate dehydrase
- beta-hydroxydecanoyl thiol ester dehydrase
- FabA
- beta-hydroxyacyl-acyl carrier protein dehydratase
- HDDase
- beta-hydroxyacyl-ACP dehydrase

reaction:
(1) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O [RN:R04414]; (2) (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein] + H2O [RN:R04416]


entry: 4.2.1.61
sysname: (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase
iubmb_reaction: R04462 > R04544
kegg_reaction: R04535 R04537 R04568 R04965
name:
--- 
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
- D-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
- beta-hydroxypalmitoyl-acyl carrier protein dehydrase
- beta-hydroxypalmitoyl thioester dehydratase
- beta-hydroxypalmityl-ACP dehydrase

comment:
Is specific for 3-hydroxyacyl-[acyl-carrier protein] derivatives (C12 to C16), and has the highest activity on the C16 derivative.

reaction:
(3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O [RN:R04462]


entry: 4.2.1.65
sysname: L-asparagine hydro-lyase
reaction: L-asparagine = 3-cyanoalanine + H2O [RN:R01267]
iubmb_reaction: R01267
name:
--- 
- 3-cyanoalanine hydratase
- beta-Cyanoalanine Hydrolase
- beta-Cyanoalanine hydratase
- beta-CNAla hydrolase
- beta-CNA nitrilase


entry: 4.2.1.70
sysname: uracil hydro-lyase (adding D-ribose 5-phosphate)
reaction: uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H2O [RN:R01055]
iubmb_reaction: R01055
name:
--- 
- pseudouridylate synthase
- pseudouridylic acid synthetase
- pseudouridine monophosphate synthetase
- 5-ribosyluracil 5-phosphate synthetase
- pseudouridylate synthetase
- psiUMP synthetase


entry: 4.2.1.71
name: --- - Deleted entry
comment:
Deleted entry: acetylenecarboxylate hydratase. This enzyme is identical to EC 4.2.1.27, acetylenecarboxylate hydratase (EC 4.2.1.71 created 1978, modified 1989, modified 2000, deleted 2004)


entry: 4.2.1.72
name: --- - Transferred to 4.1.1.78
comment:
Transferred entry: acetylenedicarboxylate hydratase. Now EC 4.1.1.78, acetylenedicarboxylate decarboxylase (EC 4.2.1.72 created 1978, deleted 2000)


entry: 4.2.1.73
sysname: protoaphin-aglucone hydro-lyase (cyclizing)
comment: The product is converted non-enzymically to erythroaphin, an aphid pigment.
reaction: protoaphin aglucone = xanthoaphin + H2O [RN:R03742]
iubmb_reaction: R03742
name:
--- 
- protoaphin-aglucone dehydratase (cyclizing)
- protoaphin dehydratase
- protoaphin dehydratase (cyclizing)


entry: 4.2.1.74
name: --- - long-chain-enoyl-CoA hydratase - long-chain enoyl coenzyme A hydratase
sysname: long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O [RN:R02685]
iubmb_reaction: R02685 > R04170 R04738 R04740 R04744 R04746 R04749
comment:
Acts in the reverse direction. The best substrate is oct-3-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA.


entry: 4.2.1.75
sysname: hydroxymethylbilane hydro-lyase (cyclizing)
reaction: hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
iubmb_reaction: R03165
name:
--- 
- uroporphyrinogen-III synthase
- porphobilinogenase
- uroporphyrinogen isomerase
- uroporphyrinogen III cosynthase
- URO-synthase

comment:
In the presence of EC 2.5.1.61, hydroxymethylbilane synthase, the enzyme forms uroporphyrinogen III from porphobilinogen.


entry: 4.2.1.78
name: --- - (S)-norcoclaurine synthase - (S)-norlaudanosoline synthase
sysname: 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine)
iubmb_reaction: R04305
kegg_reaction: R04084
comment:
The reaction makes a six-membered ring by forming a bond between C-6 of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the aldehyde in the imine formed between the substrates. The product is the precursor of the benzylisoquinoline alkaloids in plants. The enzyme, formerly known as (S)-norlaudanosoline synthase, will also catalyse the reaction of 4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but this alkaloid has not been found to occur in plants.

reaction:
4-(2-aminoethyl)benzene-1,2-diol + 4-hydroxyphenylacetaldehyde = (S)-norcoclaurine + H2O [RN:R04305]


entry: 4.2.1.80
sysname: 4-hydroxy-2-oxopentanoate hydro-lyase
comment: Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer.
reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O [RN:R02601]
iubmb_reaction: R02601
kegg_reaction: R04781 R05297 R05864
name:
--- 
- 2-oxopent-4-enoate hydratase
- 2-keto-4-pentenoate hydratase
- OEH 2-keto-4-pentenoate (vinylpyruvate)hydratase


entry: 4.2.1.83
sysname: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase
iubmb_reaction: R04478
name:
--- 
- 4-oxalmesaconate hydratase
- 4-carboxy-2-oxohexenedioate hydratase
- 4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase
- oxalmesaconate hydratase
- gamma-oxalmesaconate hydratase

reaction:
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H2O [RN:R04478]


entry: 4.2.1.84
sysname: nitrile hydro-lyase
reaction: An aliphatic amide = a nitrile + H2O [RN:R02826]
iubmb_reaction: R02826 > R02828 R04020 R05379 R05596
name:
--- 
- nitrile hydratase
- nitrilase
- 3-cyanopyridine hydratase
- NHase
- L-NHase
- H-NHase
- acrylonitrile hydratase
- aliphatic nitrile hydratase

comment:
Acts on short-chain aliphatic nitriles, converting them into the corresponding acid amides. Does not act on these amides or on aromatic nitriles. cf. EC 3.5.5.1 nitrilase.


entry: 4.2.1.86
name: --- - Deleted entry
comment:
Deleted entry: 16-dehydroprogesterone hydratase (reaction is identical to that of EC 4.2.1.98, 16alpha-hydroxyprogesterone dehydratase) (EC 4.2.1.86 created 1989, deleted 2004)


entry: 4.2.1.87
name: --- - octopamine dehydratase - octopamine hydrolyase
sysname: octopamine hydro-lyase (deaminating)
reaction: 1-(4-hydroxyphenyl)-2-aminoethanol = (4-hydroxyphenyl)acetaldehyde + NH3 [RN:R03358]
iubmb_reaction: R03358
comment:
The enzyme-catalysed reaction is believed to be dehydration to an enamine, which is spontaneously hydrolysed to an aldehyde and ammonia.


entry: 4.2.1.88
name: --- - synephrine dehydratase
sysname: 1-(4-hydroxyphenyl)-2-(methylamino)ethanol hydro-lyase (methylamine-forming)
iubmb_reaction: R03359
comment:
Removal of H2O from (+/-)-synephrine produces a 2,3-enamine, which hydrolyses to the products shown in the reaction above. The enzyme from Arthrobacter synephrinum is highly specific.

reaction:
1-(4-hydroxyphenyl)-2-(methylamino)ethanol = (4-hydroxyphenyl)acetaldehyde + methylamine [RN:R03359]


entry: 4.2.1.92
sysname: (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase
comment: Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides.
iubmb_reaction: R04521
name:
--- 
- hydroperoxide dehydratase
- hydroperoxide isomerase
- linoleate hydroperoxide isomerase
- linoleic acid hydroperoxide isomerase
- HPI

reaction:
(9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate = (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate + H2O [RN:R04521]


entry: 4.2.1.93
comment: Also acts on hydrated NADPH.
iubmb_reaction: R00129
name:
--- 
- ATP-dependent NAD(P)H-hydrate dehydratase
- reduced nicotinamide adenine dinucleotide hydrate dehydratase
- ATP-dependent H4NAD(P)OH dehydratase

sysname:
(6S)-beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleot ide hydro-lyase(ATP-hydrolysing)

reaction:
ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH [RN:R00129]


entry: 4.2.1.94
name: --- - scytalone dehydratase
sysname: scytalone 7,8-hydro-lyase
reaction: scytalone = 1,3,8-trihydroxynaphthalene + H2O [RN:R02907]
iubmb_reaction: R02907
comment:
Involved, with EC 1.1.1.252 tetrahydroxynaphthalene reductase, in the biosynthesis of melanin in pathogenic fungi.


entry: 4.2.1.95
name: --- - kievitone hydratase - KHase
sysname: kievitone-hydrate hydro-lyase
reaction: kievitone hydrate = kievitone + H2O [RN:R03622]
iubmb_reaction: R03622
comment:
The enzyme from Fusarium sp. hydrates the methylbutenyl sidechain of the isoflavonoid phytoalexins, thus reducing their toxicity.


entry: 4.2.1.96
sysname: 4a-hydroxytetrahydrobiopterin hydro-lyase
comment: catalyses the dehydration of 4a-hydroxytetrahydrobiopterins
iubmb_reaction: R04734
name:
--- 
- 4a-hydroxytetrahydrobiopterin dehydratase
- 4alpha-hydroxy-tetrahydropterin dehydratase
- pterin-4alpha-carbinolamine dehydratase

reaction:
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a- hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O [RN:R04734]


entry: 4.2.1.97
name: --- - phaseollidin hydratase
sysname: phaseollidin-hydrate hydro-lyase
reaction: phaseollidin hydrate = phaseollidin + H2O [RN:R04728]
iubmb_reaction: R04728
comment:
the enzyme from Fusarium solani, which is distinct from kievitone hydratase (EC 4.2.1.95), hydrates the methylbutenyl side-chain of the isoflavonoid phytoalexin, phaseollidin.


entry: 4.2.1.98
sysname: 16alpha-hydroxyprogesterone hydro-lyase
comment: 16alpha-Hydroxypregnenolone is also a substrate.
reaction: 16alpha-hydroxyprogesterone = 16,17-didehydroprogesterone + H2O [RN:R04166]
iubmb_reaction: R04166
kegg_reaction: R05174
name:
--- 
- 16alpha-hydroxyprogesterone dehydratase
- hydroxyprogesterone dehydroxylase
- 16alpha-hydroxyprogesterone dehydroxylase
- 16alpha-dehydroxylase


entry: 4.2.1.100
sysname: cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase
reaction: cyclohexa-1,5-dienecarbonyl-CoA + H2O = 6-hydroxycyclohex-1-enecarbonyl-CoA [RN:R05597]
iubmb_reaction: R05597
name:
--- 
- cyclohexa-1,5-dienecarbonyl-CoA hydratase
- cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
- dienoyl-CoA hydratase

comment:
Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.99.7 (glutaryl-CoA dehydrogenase), EC 1.3.99.15 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).


entry: 4.2.1.102
name: --- - Transferred to 4.2.1.100
comment:
Transferred entry: now EC 4.2.1.100 cyclohexa-1,5-diene-1-carbonyl-CoA hydratase (EC 4.2.1.102 created 2001, deleted 2001)


entry: 4.2.1.103
name: --- - cyclohexyl-isocyanide hydratase - isonitrile hydratase
sysname: N-cyclohexylformamide hydro-lyase
reaction: N-cyclohexylformamide = cyclohexyl isocyanide + H2O [RN:R05771]
iubmb_reaction: R05771
comment:
The enzyme from Pseudomonas putida strain N19-2 can also catalyse the hydration of other isonitriles to the corresponding N-substituted formamides. The enzyme has no metal requirements.


entry: 4.2.1.104
name: --- - cyanate hydratase - cyanate lyase - cyanate hydrolase - cyanase - cyanate aminohydrolase
sysname: carbamate hydro-lyase
iubmb_reaction: R07315 R07316
kegg_reaction: R03546
comment:
The enzyme requires bicarbonate as a cofactor. Its mechanism is to catalyse the attack of bicarbonate on cyanate, with elimination of carbon dioxide, thus catalysing hydration of the cyanate to carbamate. The carbamate spontaneously hydrolyses to ammonia and carbon dioxide.

reaction:
(1) cyanate (NCO-) + H2O = carbamate (H2N-CO-O-) [RN:R07315]; (2) carbamate = NH3 + CO2 (spontaneous) [RN:R07316]


entry: 4.2.1.105
name: --- - 2-hydroxyisoflavanone dehydratase
sysname: 2,7,4'-trihydroxyisoflavanone hydro-lyase
reaction: 2,7,4'-trihydroxyisoflavanone = daidzein + H2O [RN:R07317]
iubmb_reaction: R07317
kegg_reaction: R06793
comment:
Catalyses the final step in the formation of the isoflavonoid skeleton. The reaction also occurs spontaneously.


entry: 4.2.1.106
name: --- - bile-acid 7alpha-dehydratase
sysname: 7alpha,12alpha-dihydroxy-3-oxochol-4-enoate hydro-lyase
iubmb_reaction: R07318
comment:
The enzyme from Eubacterium sp. strain VPI 12708 can also use 7alpha-hydroxy-3-oxochol-4-enoate as a substrate but not 7alpha,12alpha-dihydroxy-3-oxochol-5beta-anoate, 3alpha,7alpha,12alpha-trihydroxychol-5beta-anoate or 7beta-hydroxy-3-oxochol-4-enoate.

reaction:
7alpha,12alpha-dihydroxy-3-oxochol-4-enoate = 12alpha-hydroxy-3-oxochola-4,6-dienoate + H2O [RN:R07318]


entry: 4.2.1.107
name: --- - 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase - 46 kDa hydratase 2
sysname: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-C oA hydro-lyase
iubmb_reaction: R04813
comment:
This enzyme forms part of the rat peroxisomal multifunctional enzyme perMFE-2, which also exhibits a dehydrogenase activity. The enzyme is involved in the beta-oxidation of the cholesterol side chain in the cholic-acid-biosynthesis pathway.

reaction:
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl- CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O [RN:R04813]


entry: 4.2.1.108
sysname: N4-acetyl-L-2,4-diaminobutanoate hydro-lyase
reaction: N4-acetyl-L-2,4-diaminobutanoate = L-ectoine + H2O
iubmb_reaction: (other) R06979
kegg_reaction: R06979
name:
--- 
- ectoine synthase
- N-acetyldiaminobutyrate dehydratase
- N-acetyldiaminobutanoate dehydratase
- L-ectoine synthase
- EctC

comment:
Ectoine is an osmoprotectant that is found in halophilic eubacteria. This is the third enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.6.1.76, diaminobutyrate-2-oxoglutarate transaminase and EC 2.3.1.178, diaminobutyrate acetyltransferase [1,2].


entry: 4.2.1.-
name: --- []
reaction:
(1) 3-Dehydroshikimate <=> 3,4-Dihydroxybenzoate + H2O [RN:R01627]; (2) Homocystine + 2 Cyanide <=> alpha-Amino-gamma-cyanobutanoate + Homocysteine + Thiocyanate [RN:R03730]; (3) 2-Aminomuconate + H2O <=> (Z)-5-Oxohex-2-enedioate + NH3 [RN:R03887]; (4) Glutaconyl-1-CoA + H2O <=> 2-Hydroxyglutaryl-CoA [RN:R03937]; (5) 2-Succinylbenzoate + H2O <=> 2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate [RN:R04031]; (6) 2-Oxohept-3-enedioate + H2O <=> 4-Hydroxy-2-oxo-heptanedioate [RN:R04131]; (7) 2-Oxohept-3-enedioate + H2O <=> 2,4-Dihydroxyhept-2-enedioate [RN:R04132]; (8) 4-Carboxy-4-hydroxy-2-oxoadipate <=> 4-Carboxy-2-hydroxy-cis,cis-muconate + H2O [RN:R04399]; (9) 4-Hydroxy-4-methyl-2-oxoglutarate <=> 4-Carboxy-2-oxo-4-pentanoate + H2O [RN:R04417]; (10) 3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA + H2O <=> 3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA [RN:R04809]; (11) 3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA <=> 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA + H2O [RN:R04813]; (12) 2-Hydroxyhepta-2,4-dienedioate + H2O <=> 4-Hydroxy-2-oxo-heptanedioate [RN:R04895]; (13) Salicylaldehyde + Pyruvate <=> trans-O-Hydroxybenzylidenepyruvate [RN:R05136]; (14) Acetaldehyde <=> Acetylene + H2O [RN:R05380]; (15) E-Phenylitaconyl-CoA + H2O <=> (Hydroxymethylphenyl)succinyl-CoA [RN:R05599]; (16) Cyclohex-1-ene-1-carboxyl-CoA + H2O <=> 2-Hydroxycyclohexane-1-carboxyl-CoA [RN:R05600]; (17) 6-Carboxyhex-2-enoyl-CoA + H2O <=> 3-Hydroxypimeloyl-CoA [RN:R05601]; (18) 6-Hydroxycyclohex-1-enecarbonyl-CoA + H2O <=> 2,6-Dihydroxycyclohexane-1-carboxyl-CoA [RN:R05602]; (19) Perillyl-CoA + H2O <=> 2-Hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA [RN:R06369]; (20) 2-Hydroxyhepta-2,4-dienedioate + H2O <=> 2,4-Dihydroxyhept-2-enedioate [RN:R06897]; (21) Naphthyl-2-methylene-succinyl-CoA + H2O <=> Naphthyl-2-hydroxymethyl-succinyl CoA [RN:R06906]; (22) 2-Hydroxy-3-methylbenzalpyruvate + H2O <=> 3-Methylsalicylaldehyde + Pyruvate [RN:R06913]; (23) 2-Hydroxy-3-carboxybenzalpyruvate + H2O <=> 3-Formylsalicylic acid + Pyruvate [RN:R06923]; (24) 2-Hydroxy-4-hydroxymethylbenzalpyruvate + H2O <=> 4-Hydroxymethylsalicylaldehyde + Pyruvate [RN:R06934]


entry: 4.2.2.1
sysname: hyaluronate lyase
iubmb_reaction: R02465 R06242(G)
name:
--- 
- hyaluronate lyase
- hyaluronidase [but cf. EC 3.2.1.35 (hyalurononglucosaminidase) and EC 3.2.1.36 (hyaluronoglucuronidase)]
- glucuronoglycosaminoglycan lyase
- spreading factor
- mucinase

comment:
Also acts on chondroitin. Formerly EC 4.2.99.1. The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose

reaction:
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine [RN:R02465 R06242]


entry: 4.2.2.2
sysname: (1->4)-alpha-D-galacturonan lyase
iubmb_reaction: R02361 R06240(G)
name:
--- 
- pectate lyase
- polygalacturonic transeliminase
- pectic acid transeliminase
- polygalacturonate lyase
- endopectin methyltranseliminase
- pectate transeliminase
- endogalacturonate transeliminase
- pectic acid lyase
- pectic lyase
- alpha-1,4-D-endopolygalacturonic acid lyase
- PGA lyase
- PPase-N
- endo-alpha-1,4-polygalacturonic acid lyase
- polygalacturonic acid lyase
- pectin trans-eliminase
- Polygalacturonic acid trans-eliminase

comment:
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase). Formerly EC 4.2.99.3.

reaction:
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends [RN:R02361 R06240]


entry: 4.2.2.3
sysname: poly(beta-D-1,4-mannuronide) lyase
comment: Formerly EC 4.2.99.4.
iubmb_reaction: (other) R03706
kegg_reaction: R03706
name:
--- 
- poly(beta-D-mannuronate) lyase
- alginate lyase I
- alginate lyase
- alginase I
- alginase II
- alginase

reaction:
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends


entry: 4.2.2.4
name: --- - Transferred to 4.2.2.20 and 4.2.2.21
comment:
Transferred entry: chondroitin ABC lyase. Now known to comprise two enzymes: EC 4.2.2.20, chondroitin-sulfate-ABC endolyase and EC 4.2.2.21, chondroitin-sulfate-ABC exolyase. (EC 4.2.2.4 created 1972 (EC 4.2.99.6 created 1965, part incorporated 1976), deleted 2006)


entry: 4.2.2.5
sysname: chondroitin AC lyase
name:
--- 
- chondroitin AC lyase
- chondroitinase (ambiguous)
- chondroitin sulfate lyase
- chondroitin AC eliminase
- chondroitinase AC
- ChnAC

comment:
Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [4].

reaction:
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups


entry: 4.2.2.6
sysname: oligogalacturonide lyase
iubmb_reaction: R00064 R06252(G)
kegg_reaction: R04382 R06249(G)
name:
--- 
- oligogalacturonide lyase
- oligogalacturonate lyase
- unsaturated oligogalacturonate transeliminase
- OGTE

comment:
Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.

reaction:
4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate [RN:R00064 R06252]


entry: 4.2.2.7
name: --- - heparin lyase - heparin eliminase - heparinase
sysname: heparin lyase
reaction:
Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends


entry: 4.2.2.8
sysname: heparin-sulfate lyase
comment: Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages.
name:
--- 
- heparin-sulfate lyase
- heparin-sulfate eliminase
- heparitin-sulfate lyase
- heparitinase I
- heparitinase II

reaction:
Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.


entry: 4.2.2.9
sysname: (1->4)-alpha-D-galacturonan reducing-end-disaccharide-lyase
name:
--- 
- pectate disaccharide-lyase
- pectate exo-lyase
- exopectic acid transeliminase
- exopectate lyase
- exopolygalacturonic acid-trans-eliminase
- PATE
- exo-PATE
- exo-PGL

reaction:
Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin


entry: 4.2.2.10
sysname: (1->4)-6-O-methyl-alpha-D-galacturonan lyase
name:
--- 
- pectin lyase
- pectin trans-eliminase
- endo-pectin lyase
- polymethylgalacturonic transeliminase
- pectin methyltranseliminase
- pectolyase
- PL
- PNL
- PMGL

comment:
Favours pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2, pectate lyase). Demethylation progressively slows its action; it can nevertheless cleave on either side of a demethylated residue if the residue at the other end of the scissile bond is methylated.

reaction:
Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends


entry: 4.2.2.11
sysname: poly(alpha-L-1,4-guluronide) exo-lyase
name:
--- 
- poly(alpha-L-guluronate) lyase
- alginase II
- guluronate lyase
- L-guluronan lyase
- L-guluronate lyase
- poly-alpha-L-guluronate lyase
- polyguluronate-specific alginate lyase

reaction:
Eliminative cleavage of polysaccharides containing a terminal alpha-L-guluronate group, to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends


entry: 4.2.2.12
name: --- - xanthan lyase
sysname: xanthan lyase
reaction:
Eliminative cleavage of the terminal beta-D-mannosyl-beta-D-1,4-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain


entry: 4.2.2.13
sysname: (1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
reaction: linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
name:
--- 
- exo-(1->4)-alpha-D-glucan lyase
- alpha-(1->4)-glucan 1,5-anhydro-D-fructose eliminase
- alpha-1,4-glucan exo-lyase
- alpha-1,4-glucan lyase

comment:
The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1->6)-alpha-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin.


entry: 4.2.2.14
name: --- - glucuronan lyase - (1,4)-beta-D-glucuronan lyase
sysname: (1->4)-beta-D-glucuronan lyase
reaction:
Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.


entry: 4.2.2.15
sysname: glycoconjugate sialyl-lyase (2,7-cyclizing)
name:
--- 
- anhydrosialidase
- anhydroneuraminidase
- sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing)
- sialidase L

comment:
Also acts on N-glycolylneuraminate glycosides. cf. EC 3.2.1.18 (exo-alpha-sialidase) and EC 3.2.1.129 (endo-alpha-sialidase).

reaction:
Elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate


entry: 4.2.2.16
sysname: 2,6-beta-D-fructan lyase (di-beta-D-fructofuranose-2,6':2',6-dianhydride-forming)
name:
--- 
- levan fructotransferase (DFA-IV-forming)
- 2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming di-beta-D-fructofuranose 2,6':2',6-dianhydride)
- levan fructotransferase

comment:
This enzyme, like EC 4.2.2.17 [inulin fructotransferase (DFA-I-forming)] and EC 4.2.2.18 [inulin fructotransferase (DFA-III-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.

reaction:
Produces di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide


entry: 4.2.2.17
name:
--- 
- inulin fructotransferase (DFA-I-forming)
- inulin fructotransferase (DFA-I-producing)
- inulin fructotransferase (depolymerizing, difructofuranose-1,2':2',1-dianhydride-forming)
- inulin D-fructosyl-D-fructosyltransferase (1,2':1',2-dianhydride-forming)
- inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':1',2-dianhydride)

sysname:
2,1-beta-D-fructan lyase (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,1'-dianhydride- forming)

comment:
This enzyme, like EC 4.2.2.16 [levan fructotransferase (DFA-IV-forming)] and EC 4.2.2.18 [inulin fructotransferase (DFA-III-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.

reaction:
Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.


entry: 4.2.2.18
name:
--- 
- inulin fructotransferase (DFA-III-forming)
- inulin fructotransferase (DFA-III-producing)
- inulin fructotransferase (depolymerizing)
- inulase II
- inulinase II
- inulin fructotransferase (depolymerizing, difructofuranose-1,2':2,3'-dianhydride-forming)
- inulin D-fructosyl-D-fructosyltransferase (1,2':2,3'-dianhydride-forming)
- inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride)

sysname:
2,1-beta-D-fructan lyase (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,3'-dianhydride- forming)

comment:
This enzyme, like EC 4.2.2.16 [levan fructotransferase (DFA-IV-forming)] and EC 4.2.2.17 [inulin fructotransferase (DFA-I-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the common name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.

reaction:
Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.


entry: 4.2.2.19
name: --- - chondroitin B lyase - chondroitinase B - ChonB - ChnB
sysname: chondroitin B lyase
comment:
This is the only lyase that is known to be specific for dermatan sulfate as substrate. The minimum substrate length required for catalysis is a tetrasaccharide [2]. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5].

reaction:
Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAC-4S).


entry: 4.2.2.20
sysname: chondroitin-sulfate-ABC endolyase
name:
--- 
- chondroitin-sulfate-ABC endolyase
- chondroitinase (ambiguous)
- chondroitin ABC eliminase (ambiguous)
- chondroitinase ABC (ambiguous)
- chondroitin ABC lyase (ambiguous)
- chondroitin sulfate ABC lyase (ambiguous)
- ChS ABC lyase (ambiguous)
- chondroitin sulfate ABC endoeliminase
- chondroitin sulfate ABC endolyase
- ChS ABC lyase I

comment:
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5]. The related enzyme EC 4.2.2.21, chondroitin-sulfate-ABC exolyase, has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20 [4].

reaction:
Endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides


entry: 4.2.2.21
sysname: chondroitin-sulfate-ABC exolyase
name:
--- 
- chondroitin-sulfate-ABC exolyase
- chondroitinase (ambiguous)
- chondroitin ABC eliminase (ambiguous)
- chondroitinase ABC (ambiguous)
- chondroitin ABC lyase (ambiguous)
- chondroitin sulfate ABC lyase (ambiguous)
- ChS ABC lyase (ambiguous)
- chondroitin sulfate ABC exoeliminase
- chondroitin sulfate ABC exolyase
- ChS ABC lyase II

comment:
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5]. The related enzyme EC 4.2.2.20, chondroitin-sulfate-ABC endolyase, has the same substrate specificity but produces a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides [4].

reaction:
Exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments


entry: 4.2.3.2
sysname: ethanolamine-phosphate phospho-lyase (deaminating)
comment: A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
reaction: ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate [RN:R00748]
iubmb_reaction: R00748
name:
--- 
- ethanolamine-phosphate phospho-lyase
- O-phosphoethanolamine-phospholyase
- amino alcohol O-phosphate phospholyase
- O-phosphorylethanol-amine phospho-lyase


entry: 4.2.3.4
sysname: 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing)
reaction: 3-deoxy-arabino-heptulonate 7-phosphate = 3-dehydroquinate + phosphate [RN:R03083]
iubmb_reaction: R03083
name:
--- 
- 3-dehydroquinate synthase
- 5-dehydroquinate synthase
- 5-dehydroquinic acid synthetase
- dehydroquinate synthase
- 3-dehydroquinate synthetase
- 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing)

comment:
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.


entry: 4.2.3.5
name: --- - chorismate synthase
sysname: 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
reaction: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate [RN:R01714]
iubmb_reaction: R01714
comment:
Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH*). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.


entry: 4.2.3.6
sysname: trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
reaction: trans,trans-farnesyl diphosphate = trichodiene + diphosphate [RN:R02306]
iubmb_reaction: R02306
kegg_reaction: R02310
name:
--- 
- trichodiene synthase
- trichodiene synthetase
- sesquiterpene cyclase
- trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase


entry: 4.2.3.7
name: --- - pentalenene synthase - pentalenene synthetase
sysname: 2-trans,6-trans-farnesyldiphosphate diphosphate-lyase (cyclizing, pentalenene-forming)
reaction: 2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate [RN:R02305]
iubmb_reaction: R02305
comment:
The initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.


entry: 4.2.3.8
sysname: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, CASbene-forming)
comment: The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene.
reaction: geranylgeranyl diphosphate = casbene + diphosphate [RN:R02064]
iubmb_reaction: R02064
name:
--- 
- casbene synthase
- casbene synthetase
- geranylgeranyl-diphosphate diphosphate-lyase (cyclizing)


entry: 4.2.3.9
sysname: 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)
reaction: 2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate [RN:R02307]
iubmb_reaction: R02307
name:
--- 
- aristolochene synthase
- sesquiterpene cyclase
- trans,trans-farnesyl diphosphate aristolochene-lyase
- trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)

comment:
The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti [5] (see also EC 4.2.3.23, germacrene-A synthase). The enzyme from Penicillium roqueforti requires Mg2+ and Mn2+ for activity. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.


entry: 4.2.3.10
sysname: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-endo-fenchol-forming]
comment: (3R)-Linalyl diphosphate is an intermediate in the reaction
reaction: geranyl diphosphate + H2O = (-)-endo-fenchol + diphosphate [RN:R02004]
iubmb_reaction: R02004
name:
--- 
- (-)-endo-fenchol synthase
- (-)-endo-fenchol cyclase
- geranyl pyrophosphate:(-)-endo-fenchol cyclase


entry: 4.2.3.11
name: --- - sabinene-hydrate synthase - sabinene hydrate cyclase
sysname: geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate-forming)
reaction: geranyl diphosphate + H2O = sabinene hydrate + diphosphate [RN:R02006]
iubmb_reaction: R02006
comment:
Both cis- and trans- isomers of sabinene hydrate are formed. (3R)-Linalyl diphosphate is an intermediate in the reaction


entry: 4.2.3.12
name: --- - 6-pyruvoyltetrahydropterin synthase
iubmb_reaction: R04286
kegg_reaction: R04735
sysname:
2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-di hydroxypteridine triphosphate lyase

comment:
catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. The product is 6-pyruvoyltetrahydrobiopterin.

reaction:
6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate [RN:R04286]


entry: 4.2.3.13
name: --- - (+)-delta-cadinene synthase
sysname: 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-delta-cadinene-forming)
reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-delta-cadinene + diphosphate [RN:R02311]
iubmb_reaction: R02311
comment:
the sesquiterpenoid (+)-delta-cadinene is an intermediate in phytoalexin biosynthesis. Mg2+ is required for activity.


entry: 4.2.3.14
sysname: geranyl-diphosphate diphosphate-lyase (cyclizing, pinene-forming)
reaction: geranyl diphosphate = pinene + diphosphate [RN:R02012]
iubmb_reaction: R02012 > R05765 R05766
name:
--- 
- pinene synthase
- beta-geraniolene synthase
- (-)-(1S,5S)-pinene synthase
- geranyldiphosphate diphosphate lyase (pinene forming)

comment:
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor. A mixture of alpha and beta-pinene is produced.


entry: 4.2.3.15
name: --- - myrcene synthase
sysname: geranyl-diphosphate diphosphate-lyase (myrcene-forming)
reaction: geranyl diphosphate = myrcene + diphosphate [RN:R02009]
iubmb_reaction: R02009
comment:
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.


entry: 4.2.3.16
sysname: geranyldiphosphate diphosphate lyase [cyclizing, (4S)-limonene-forming]
reaction: geranyl diphosphate = (-)-(4S)-limonene + diphosphate [RN:R02013]
iubmb_reaction: R02013
name:
--- 
- (4S)-limonene synthase
- (-)-(4S)-limonene synthase
- 4S-(-)-limonene synthase
- geranyldiphosphate diphosphate lyase (limonene forming)

comment:
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.


entry: 4.2.3.18
sysname: copalyl-diphosphate diphosphate-lyase (cyclizing)
reaction: (+)-copalyl diphosphate = (-)-abietadiene + diphosphate [RN:R06301]
iubmb_reaction: R06301
kegg_reaction: R06299 R06300 R06302 R06303 R06304
name:
--- 
- abietadiene synthase
- copalyl-diphosphate diphosphate-lyase (cyclizing, abietadiene-forming)

comment:
Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 5.5.1.12 (copalyl diphosphate synthase). Requires Mg2+


entry: 4.2.3.19
sysname: ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming)
reaction: ent-copalyl diphosphate = ent-kaurene + diphosphate [RN:R05092]
iubmb_reaction: R05092
name:
--- 
- ent-kaurene synthase
- ent-kaurene synthase B
- ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase (cyclizing)

comment:
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)


entry: 4.2.3.20
sysname: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-(4R)-limonene-forming]
reaction: geranyl diphosphate = (+)-(4R)-limonene + diphosphate [RN:R06120]
iubmb_reaction: R06120
name:
--- 
- (R)-limonene synthase
- (+)-limonene synthase
- geranyldiphosphate diphosphate lyase [(+)-(R)-limonene-forming]

comment:
Forms the first step of carvone biosynthesis in caraway. The enzyme from Carum carvi (caraway) seeds requires a divalent metal ion (preferably Mn2+) for catalysis. This enzyme occurs in Citrus, Carum (caraway) and Anethum (dill); (-)-limonene, however, is made in the fir, Abies, and mint, Mentha, by EC 4.2.3.16, (4S)-limonene synthase.


entry: 4.2.3.21
sysname: trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, vetispiradiene-forming)
comment: The initial internal cyclization produces the monocyclic intermediate germacrene A.
reaction: trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate [RN:R06523]
iubmb_reaction: R06523
name:
--- 
- vetispiradiene synthase
- vetispiradiene-forming farnesyl pyrophosphate cyclase
- pemnaspirodiene synthase
- HVS
- vetispiradiene cyclase


entry: 4.2.3.22
name: --- - germacradienol synthase - germacradienol/germacrene-D synthase
sysname:
2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]

comment:
Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate [2]. Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin, a widely occurring metabolite of many streptomycetes, bacteria and fungi [2].

reaction:
(1) 2-trans,6-trans-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate; (2) 2-trans,6-trans-farnesyl diphosphate = (-)-(7S)-germacrene D + diphosphate


entry: 4.2.3.23
sysname: 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (germacrene-A-forming)
reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate
name:
--- 
- germacrene-A synthase
- germacrene A synthase
- (+)-germacrene A synthase
- (+)-(10R)-germacrene A synthase
- GAS

comment:
Requires Mg2+ for activity. While germacrene A is an enzyme-bound intermediate in the biosynthesis of a number of phytoalexins, e.g. EC 4.2.3.9 (aristolochene synthase) from some species and EC 4.2.3.21 (vetispiradiene synthase), it is the sole sesquiterpenoid product formed in chicory [1].


entry: 4.2.3.24
name: --- - amorpha-4,11-diene synthase - amorphadiene synthase
sysname: 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (amorpha-4,11-diene-forming)
reaction: 2-trans,6-trans-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
comment:
Requires Mg2+ and Mn2+ for activity. This is a key enzyme in the biosynthesis of the antimalarial endoperoxide artemisinin [3]. Catalyses the formation of both olefinic [e.g. amorpha-4,11-diene, amorpha-4,7(11)-diene, gamma-humulene and beta-sesquiphellandrene] and oxygenated (e.g. amorpha-4-en-7-ol) sesquiterpenes, with amorpha-4,11-diene being the major product. When geranyl diphosphate is used as a substrate, no monoterpenes are produced [2].


entry: 4.2.3.25
name: --- - S-linalool synthase - LIS - Lis - 3S-linalool synthase
sysname: geranyl-diphosphate diphosphate-lyase [(3S)-linalool-forming]
reaction: geranyl diphosphate + H2O = (3S)-linalool + diphosphate
comment:
Requires Mn2+ or Mg2+ for activity. Neither (3S)- nor (3R)-linalyl diphosphate can act as substrate for the enzyme from the flower Clarkia breweri [1]. Unlike many other monoterpene synthases, only a single product, (3S)-linalool, is formed.


entry: 4.2.3.26
name: --- - R-linalool synthase - (3R)-linalool synthase - (-)-3R-linalool synthase
sysname: geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]
reaction: geranyl diphosphate + H2O = (3R)-linalool + diphosphate
comment:
Geranyl diphosphate cannot be replaced by isopentenyl diphosphate, dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate [1]. Requires Mg2+ or Mn2+ for activity. Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed.


entry: 4.2.99.6
name: --- - Deleted entry
comment:
Deleted entry: chondroitin sulfate lyase. Now included with EC 4.2.2.4 (chondroitin ABC lyase) and EC 4.2.2.5 (chondroitin AC lyase) (EC 4.2.99.6 created 1965, deleted 1972)


entry: 4.2.99.7
name: --- - Transferred to 4.2.3.2
comment:
Transferred entry: now EC 4.2.3.2, ethanolamine-phosphate phospho-lyase (EC 4.2.99.7 created 1972, deleted 2000)


entry: 4.2.99.8
name: --- - Transferred to 2.5.1.47
comment:
Transferred entry: now EC 2.5.1.47, cysteine synthase (EC 4.2.99.8 created 1972, modified 1976, modified 1990, deleted 2002)


entry: 4.2.99.9
name: --- - Transferred to 2.5.1.48
comment:
Transferred entry: now EC 2.5.1.48, cystathionine gamma-synthase (EC 4.2.99.9 created 1972, deleted 2002)


entry: 4.2.99.10
name: --- - Transferred to 2.5.1.49
comment:
Transferred entry: now EC 2.5.1.49, O-acetylhomoserine aminocarboxypropyltransferase (EC 4.2.99.10 created 1972, deleted 2002)


entry: 4.2.99.13
name: --- - Transferred to 2.5.1.50
comment:
Transferred entry: now EC 2.5.1.50, zeatin 9-aminocarboxyethyltransferase (EC 4.2.99.13 created 1984, deleted 2002)


entry: 4.2.99.14
name: --- - Transferred to 2.5.1.51
comment:
Transferred entry: now EC 2.5.1.51, beta-pyrazolylalanine synthase (EC 4.2.99.14 created 1989 (EC 4.2.99.17 incorporated 1992), deleted 2002)


entry: 4.2.99.16
name: --- - Transferred to 2.5.1.53
comment:
Transferred entry: now EC 2.5.1.53, uracilylalanine synthase (EC 4.2.99.16 created 1990, deleted 2002)


entry: 4.2.99.17
name: --- - Deleted entry
comment:
Deleted entry: listed as EC 4.2.99.14 beta-pyrazolylalanine synthase (acetylserine) (EC 4.2.99.17 created 1992, deleted 1992)


entry: 4.2.99.18
sysname: DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
name:
--- 
- DNA-(apurinic or apyrimidinic site) lyase
- AP lyase
- AP endonuclease class I
- endodeoxyribonuclease (apurinic or apyrimidinic)
- deoxyribonuclease (apurinic or apyrimidinic)
- E. coli endonuclease III
- phage-T4 UV endonuclease
- Micrococcus luteus UV endonuclease
- AP site-DNA 5'-phosphomonoester-lyase
- X-ray endonuclease III

comment:
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.

reaction:
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate


entry: 4.2.99.19
name: --- - Transferred to 4.4.1.23
comment:
Transferred entry: Now EC 4.4.1.23, 2-hydroxypropyl-CoM lyase. The enzyme was incorrectly classified as acting on a C-O bond rather than a C-S bond (EC 4.2.99.19 created 2001, deleted 2005)


entry: 4.3.1.4
name: --- - formimidoyltetrahydrofolate cyclodeaminase - formiminotetrahydrofolate cyclodeaminase
sysname: 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing)
reaction: 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3 [RN:R02302]
iubmb_reaction: R02302
comment:
In eukaroytes, occurs as a bifunctional enzyme that also has glutamate formimidoyltransferase (EC 2.1.2.5) activity.


entry: 4.3.1.5
sysname: L-phenylalanine ammonia-lyase
comment: This enzyme may also act on L-tyrosine.
reaction: L-phenylalanine = trans-cinnamate + NH3 [RN:R00697]
iubmb_reaction: R00697
kegg_reaction: R00737 R06132
name:
--- 
- phenylalanine ammonia-lyase
- tyrase
- phenylalanine deaminase
- tyrosine ammonia-lyase
- L-tyrosine ammonia-lyase
- phenylalanine ammonium-lyase
- PAL


entry: 4.3.1.8
name: --- - Transferred to 2.5.1.61
comment:
Transferred entry: now EC 2.5.1.61 hydroxymethylbilane synthase. (EC 4.3.1.8 created 1972, deleted 2003)


entry: 4.3.1.9
sysname: D-glucosaminate ammonia-lyase (isomerizing)
comment: Contains pyridoxal phosphate.
reaction: D-glucosaminate = 2-dehydro-3-deoxy-D-gluconate + NH3 [RN:R01544]
iubmb_reaction: R01544
kegg_reaction: R06132
name:
--- 
- glucosaminate ammonia-lyase
- glucosaminic dehydrase
- D-glucosaminate dehydratase
- D-glucosaminic acid dehydrase
- aminodeoxygluconate dehydratase
- 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating)
- aminodeoxygluconate ammonia-lyase
- 2-amino-2-deoxy-D-gluconate ammonia-lyase


entry: 4.3.1.11
sysname: 3,4-dihydroxy-L-phenylalanine ammonia-lyase
reaction: 3,4-dihydroxy-L-phenylalanine = trans-caffeate + NH3 [RN:R02079]
iubmb_reaction: R02079
kegg_reaction: R06132
name:
--- 
- dihydroxyphenylalanine ammonia-lyase
- beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase


entry: 4.3.1.12
name: --- - ornithine cyclodeaminase - ornithine cyclase - ornithine cyclase (deaminating)
sysname: L-ornithine ammonia-lyase (cyclizing)
reaction: L-ornithine = L-proline + NH3 [RN:R00671]
iubmb_reaction: R00671
comment:
Requires NAD+. The enzyme is a member of the mu-crystallin protein family [4]. The reaction is stimulated by the presence of ADP or ATP and is inhibited by O2 [2].


entry: 4.3.1.14
name: --- - 3-aminobutyryl-CoA ammonia-lyase - L-3-aminobutyryl-CoA deaminase
sysname: L-3-aminobutyryl-CoA ammonia-lyase
reaction: L-3-aminobutyryl-CoA = crotonoyl-CoA + NH3 [RN:R03030]
iubmb_reaction: R03030
comment:
hydroxylamine can replace ammonia as a substrate. Crotonoyl-pantetheine can replace crotonoyl-CoA but it is a poorer substrate.


entry: 4.3.1.15
sysname: 2,3-diaminopropanoate ammonia-lyase
reaction: 2,3-diaminopropanoate + H2O = pyruvate + 2 NH3 [RN:R00195]
iubmb_reaction: R00195
kegg_reaction: R00223
name:
--- 
- diaminopropionate ammonia-lyase
- diaminopropionatase
- alpha,beta-diaminopropionate ammonia-lyase
- 2,3-diaminopropionate ammonia-lyase

comment:
a pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates.


entry: 4.3.1.16
sysname: threo-3-hydroxy-L-aspartate ammonia-lyase
comment: A pyridoxal-phosphate protein.
reaction: threo-3-hydroxy-L-aspartate = oxaloacetate + NH3 [RN:R05758]
iubmb_reaction: R05758
name:
--- 
- threo-3-hydroxyaspartate ammonia-lyase
- threo-3-hydroxyaspartate dehydratase
- L-threo-3-hydroxyaspartate dehydratase


entry: 4.3.1.17
sysname: L-serine ammonia-lyase
reaction: L-serine = pyruvate + NH3 [RN:R00220]
iubmb_reaction: R00220
kegg_reaction: R00590 R06131
name:
--- 
- L-serine ammonia-lyase
- serine deaminase
- L-hydroxyaminoacid dehydratase
- L-serine deaminase
- L-serine dehydratase
- L-serine hydro-lyase (deaminating)

comment:
A pyridoxal-phosphate protein. This reaction is also carried out by EC 4.3.1.19 threonine ammonia-lyase, from a number of sources. The reaction catalysed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by isomerization and hydrolysis of the product with C-N bond breakage.


entry: 4.3.1.18
sysname: D-serine ammonia-lyase
reaction: D-serine = pyruvate + NH3 [RN:R00221]
iubmb_reaction: R00221
kegg_reaction: R06131
name:
--- 
- D-serine ammonia-lyase
- D-hydroxyaminoacid dehydratase
- D-serine dehydrase
- D-hydroxy amino acid dehydratase
- D-serine hydrolase
- D-serine dehydratase (deaminating)
- D-serine deaminase
- D-serine hydro-lyase (deaminating)

comment:
A pyridoxal-phosphate protein. Also acts, slowly, on D-threonine. The reaction catalysed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase), followed by isomerization and hydrolysis of the product with C-N bond breakage.


entry: 4.3.1.19
sysname: L-threonine ammonia-lyase
reaction: L-threonine = 2-oxobutanoate + NH3 [RN:R00996]
iubmb_reaction: R00996
kegg_reaction: R00220 R06131
name:
--- 
- threonine ammonia-lyase
- threonine deaminase
- L-serine dehydratase
- serine deaminase
- L-threonine dehydratase
- threonine dehydrase
- L-threonine deaminase
- threonine dehydratase
- L-threonine hydro-lyase (deaminating)

comment:
The enzyme from many sources is a pyridoxal-phosphate protein; that from Pseudomonas putida is not. The enzyme from a number of sources also acts on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase. The reaction catalysed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by isomerization and hydrolysis of the product with C-N bond breakage.


entry: 4.3.1.20
sysname: erythro-3-hydroxy-L(s)-aspartate ammonia-lyase
reaction: erythro-3-hydroxy-L-aspartate = oxaloacetate + NH3 [RN:R00347]
iubmb_reaction: R00347
kegg_reaction: R06131
name:
--- 
- erythro-3-hydroxyaspartate ammonia-lyase
- 3-hydroxyaspartate dehydratase
- erythro-beta-hydroxyaspartate dehydratase
- erythro-3-hydroxyaspartate dehydratase
- erythro-3-hydroxy-L(s)-aspartate hydro-lyase (deaminating)

comment:
A pyridoxal-phosphate protein. The reaction catalysed probably involves initial elimination of water (hence the enzyme's original classification as EC 4.2.1.38, erythro-3-hydroxyaspartate dehydratase), followed by isomerization and hydrolysis of the product with C-N bond breakage.


entry: 4.3.1.21
name: --- - Deleted entry
comment:
Deleted entry: aminodeoxygluconate ammonia-lyase. Enzyme is identical to EC 4.3.1.9, glucosaminate ammonia-lyase (EC 4.3.1.21 created 1965 as EC 4.2.1.26, transferred 2002 to EC 4.3.1.21, deleted 2004)


entry: 4.3.2.1
sysname: N-(L-argininosuccinate) arginine-lyase
reaction: (N(omega)-L-arginino)succinate = fumarate + L-arginine [RN:R01086]
iubmb_reaction: R01086
name:
--- 
- argininosuccinate lyase
- arginosuccinase
- argininosuccinic acid lyase
- arginine-succinate lyase


entry: 4.3.2.2
name: --- - adenylosuccinate lyase - adenylosuccinase - succino AMP-lyase
sysname: N6-(1,2-dicarboxyethyl)AMP AMP-lyase
comment: Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
iubmb_reaction: R01083 R04559
reaction:
(1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP [RN:R01083]; (2) (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [RN:R04559]


entry: 4.3.2.4
name: --- - purine imidazole-ring cyclase
sysname: DNA-4,6-diamino-5-formamidopyrimidine C8-N9-lyase (cyclizing)
reaction: DNA 4,6-diamino-5-formamidopyrimidine = DNA adenine + H2O [RN:R02960]
iubmb_reaction: R02960
comment:
Also acts on 2,6-diamino-5-formamido-3,4-dihydro-4-oxopyrimidine residues. Brings about the reclosure of the imidazole rings of purine residues damaged by gamma-rays.


entry: 4.3.2.5
sysname: peptidylamidoglycolate peptidylamide-lyase
reaction: peptidylamidoglycolate = peptidyl amide + glyoxylate [RN:R03874]
iubmb_reaction: R03874
name:
--- 
- peptidylamidoglycolate lyase
- alpha-hydroxyglycine amidating dealkylase
- peptidyl-alpha-hydroxyglycine alpha-amidating lyase
- HGAD
- PGL
- PAL

comment:
The enzyme acts on the product of the reaction catalysed by EC 1.14.17.3 peptidylglycine monooxygenase, thus removing a terminal glycine residue and leaving a des-glycine peptide amide.


entry: 4.3.3.1
sysname: 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase
iubmb_reaction: R04367
name:
--- 
- 3-ketovalidoxylamine C-N-lyase
- 3-ketovalidoxylamine A C-N-lyase
- p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase

comment:
Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-alpha-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.

reaction:
4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one [RN:R04367]


entry: 4.3.3.2
name: --- - strictosidine synthase - strictosidine synthetase
sysname: 3-alpha(S)-strictosidine tryptamine-lyase
reaction: tryptamine + secologanin = 3-alpha(S)-strictosidine + H2O [RN:R03738]
iubmb_reaction: R03738
comment:
Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.


entry: 4.3.3.3
name: --- - deacetylisoipecoside synthase
sysname: deacetylisoipecoside dopamine-lyase
reaction: dopamine + secologanin = deacetylisoipecoside + H2O [RN:R05750]
iubmb_reaction: R05750
comment:
The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.4 deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.


entry: 4.3.3.4
name: --- - deacetylipecoside synthase
sysname: deacetylipecoside dopamine-lyase
reaction: dopamine + secologanin = deacetylipecoside + H2O [RN:R05749]
iubmb_reaction: R05749
comment:
The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.3 deacetylisoipecoside synthase. The product is rapidly converted to demethylalangiside.


entry: 4.3.3.-
name: --- []
reaction:
(1) Ethanolamine + Acetaldehyde <=> Diethanolamine [RN:R05381]; (2) Triethanolamine <=> Diethanolamine + Acetaldehyde [RN:R05382]


entry: 4.3.99.1
name: --- - Transferred to 4.2.1.104
comment:
Transferred entry: now EC 4.2.1.104, cyanate hydratase (EC 4.3.99.1 created 1972 as EC 3.5.5.3, transferred 1990 to EC 4.3.99.1, deleted 2001)


entry: 4.4.1.1
sysname: L-cystathionine cysteine-lyase (deaminating)
reaction: L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate [RN:R01001]
iubmb_reaction: R01001
kegg_reaction: R00782 R02408 R04930
name:
--- 
- cystathionine gamma-lyase
- homoserine deaminase
- homoserine dehydratase
- cystine desulfhydrase
- cysteine desulfhydrase
- gamma-cystathionase
- cystathionase
- homoserine deaminase-cystathionase
- gamma-CTL
- cystalysin
- cysteine lyase

comment:
A multifunctional pyridoxal-phosphate protein. Also catalyses elimination reactions of L-homoserine to form H2O, NH3 and 2-oxobutanoate, of L-cystine, producing thiocysteine, pyruvate and NH3, and of L-cysteine producing pyruvate, NH3 and H2S.


entry: 4.4.1.4
sysname: alliin alkyl-sulfenate-lyase
comment: A pyridoxal-phosphate protein.
reaction: An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate [RN:R03901]
iubmb_reaction: R03901
name:
--- 
- alliin lyase
- alliinase
- cysteine sulfoxide lyase
- alkylcysteine sulfoxide lyase
- S-alkylcysteine sulfoxide lyase
- L-cysteine sulfoxide lyase
- S-alkyl-L-cysteine sulfoxide lyase


entry: 4.4.1.5
sysname: (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing)
comment: Also acts on 3-phosphoglycerol-glutathione.
reaction: (R)-S-lactoylglutathione = glutathione + methylglyoxal [RN:R02530]
iubmb_reaction: R02530
name:
--- 
- lactoylglutathione lyase
- methylglyoxalase
- aldoketomutase
- ketone-aldehyde mutase
- glyoxylase I


entry: 4.4.1.6
sysname: S-alkyl-L-cysteine alkylthiol-lyase (deaminating)
reaction: An S-alkyl-L-cysteine + H2O = an alkyl thiol + NH3 + pyruvate [RN:R02953]
iubmb_reaction: R02953
name:
--- 
- S-alkylcysteine lyase
- S-alkylcysteinase
- alkylcysteine lyase
- S-alkyl-L-cysteine sulfoxide lyase
- S-alkyl-L-cysteine lyase
- S-alkyl-L-cysteinase
- alkyl cysteine lyase

comment:
A pyridoxal-phosphate protein. Decomposes S-alkyl-L-cysteines by alpha,beta-elimination. Possibly identical, in yeast, with EC 4.4.1.8 cystathionine beta-lyase.


entry: 4.4.1.7
name: --- - Deleted entry
comment:
Deleted entry: S-(hydroxyalkyl)glutathione lyase. Now included with EC 2.5.1.18 glutathione transferase (EC 4.4.1.7 created 1972, deleted 1976)


entry: 4.4.1.8
sysname: L-cystathionine L-homocysteine-lyase (deaminating)
reaction: L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate [RN:R01286]
iubmb_reaction: R01286
kegg_reaction: R00782 R01285 R02408 R04941
name:
--- 
- cystathionine beta-lyase
- beta-cystathionase
- cystine lyase
- cystathionine L-homocysteine-lyase (deaminating)

comment:
A pyridoxal-phosphate protein. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in yeast, with EC 4.4.1.6 S-alkylcysteine lyase.


entry: 4.4.1.9
sysname: L-cysteine hydrogen-sulfide-lyase (adding HCN)
comment: Contains pyridoxal phospate.
reaction: L-cysteine + hydrogen cyanide = sulfide + L-3-cyanoalanine [RN:R03524]
iubmb_reaction: R03524
kegg_reaction: R02846
name:
--- 
- L-3-cyanoalanine synthase
- beta-cyanoalanine synthase
- beta-cyanoalanine synthetase
- beta-cyano-L-alanine synthase


entry: 4.4.1.10
name: --- - cysteine lyase - cysteine (sulfite) lyase
sysname: L-cysteine hydrogen-sulfide-lyase (adding sulfite)
reaction: L-cysteine + sulfite = L-cysteate + sulfide [RN:R00901]
iubmb_reaction: R00901
comment:
A pyridoxal-phosphate protein. Can use a second molecule of cysteine (producing lanthionine), or other alkyl thiols, as a replacing agent.


entry: 4.4.1.11
sysname: L-methionine methanethiol-lyase (deaminating)
comment: A pyridoxal-phosphate protein.
reaction: L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate [RN:R00654]
iubmb_reaction: R00654
kegg_reaction: R04770
name:
--- 
- methionine gamma-lyase
- L-methioninase
- methionine lyase
- methioninase
- methionine dethiomethylase
- L-methionine gamma-lyase


entry: 4.4.1.12
name: --- - Deleted entry
comment:
Deleted entry: sulfoacetaldehyde lyase. Activity due to EC 2.3.3.15, sulfoacetaldehyde acetyltransferase. (EC 4.4.1.12 created 1976, deleted 2003)


entry: 4.4.1.13
sysname: L-cysteine-S-conjugate thiol-lyase (deaminating)
reaction: RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528]
iubmb_reaction: R03528
name:
--- 
- cysteine-S-conjugate beta-lyase
- cysteine conjugate beta-lyase
- glutamine transaminase K/cysteine conjugate beta-lyase

comment:
A pyridoxal-phosphate protein. In the reaction, RH may represent aromatic compounds such as 4-bromobenzene and 2,4-dinitrobenzene.


entry: 4.4.1.14
sysname: S-adenosyl-L-methionine methylthioadenosine-lyase
comment: A pyridoxal-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
reaction: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine [RN:R00179]
iubmb_reaction: R00179
name:
--- 
- 1-aminocyclopropane-1-carboxylate synthase
- 1-aminocyclopropanecarboxylate synthase
- 1-aminocyclopropane-1-carboxylic acid synthase
- 1-aminocyclopropane-1-carboxylate synthetase
- aminocyclopropanecarboxylic acid synthase
- aminocyclopropanecarboxylate synthase
- ACC synthase


entry: 4.4.1.16
name: --- - selenocysteine lyase - selenocysteine reductase - selenocysteine beta-lyase
sysname: L-selenocysteine selenide-lyase (L-alanine-forming)
reaction: L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor [RN:R03598]
iubmb_reaction: R03598
kegg_reaction: R03599
comment:
A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. The enzyme does not act on cysteine, serine or chloroalanine.


entry: 4.4.1.17
name: --- - holocytochrome-c synthase - cytochrome c heme-lyase - holocytochrome c synthetase
sysname: holocytochrome-c apocytochrome-c-lyase
reaction: holocytochrome c = apocytochrome c + heme [RN:R03902]
iubmb_reaction: R03902
kegg_reaction: R02480
comment:
In the reverse direction, the enzyme catalyses the attachment of heme to two cysteine residues in the protein, forming thioether links.


entry: 4.4.1.19
name: --- - phosphosulfolactate synthase - (2R)-phospho-3-sulfolactate synthase
sysname: (2R)-O-phospho-3-sulfolactate sulfo-lyase
reaction: (2R)-O-phospho-3-sulfolactate = sulfite + phosphoenolpyruvate
iubmb_reaction: (other) R07476
kegg_reaction: R07476
comment:
Requires Mg2+. The enzyme from Methanococcus jannaschii catalyses the Michael addition of sulfite to phosphoenolpyruvate. It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than bisulfite.


entry: 4.4.1.20
reaction: leukotriene C4 = leukotriene A4 + glutathione [RN:R03059]
iubmb_reaction: R03059
name:
--- 
- leukotriene-C4 synthase
- leukotriene C4 synthetase
- LTC4 synthase
- LTC4 synthetase
- leukotriene A4:glutathione S-leukotrienyltransferase
- (7E,9E,11Z,14Z)-(5S,6R)-5,6-epoxyicosa-7,9,11,14- tetraenoate:glutathione leukotriene-transferase (epoxide-ring-opening)

sysname:
(7E,9E,11Z,14Z)-(5S,6R)-6-(glutathion-S-yl)-5-hydroxyicosa-7,9,11,14 -tetraenoate glutathione-lyase (epoxide-forming)

comment:
The reaction proceeds in the direction of addition. Not identical with EC 2.5.1.18, glutathione transferase.


entry: 4.4.1.21
name: --- - S-ribosylhomocysteine lyase - S-ribosylhomocysteinase - LuxS
reaction: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
iubmb_reaction: (other) R01291
kegg_reaction: R01291
sysname:
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]

comment:
Contains Fe2+. The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density [2].


entry: 4.4.1.22
sysname: S-(hydroxymethyl)glutathione formaldehyde-lyase
reaction: S-(hydroxymethyl)glutathione = glutathione + formaldehyde [RN:R06982]
iubmb_reaction: R06982
name:
--- 
- S-(hydroxymethyl)glutathione synthase
- glutathione-dependent formaldehyde-activating enzyme
- Gfa

comment:
The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase, in the formaldehyde-detoxification pathway.


entry: 4.4.1.23
sysname: (R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
reaction: (R)-[or (S)-]2-hydroxypropyl-CoM = (R)-[or (S)-]1,2-epoxypropane + HS-CoM [RN:R05761 R05762]
iubmb_reaction: R05761 R05762
name:
--- 
- 2-hydroxypropyl-CoM lyase
- epoxyalkane:coenzyme M transferase
- epoxyalkane:CoM transferase
- epoxyalkane:2-mercaptoethanesulfonate transferase
- coenzyme M-epoxyalkane ligase
- epoxyalkyl:CoM transferase
- epoxypropane:coenzyme M transferase
- epoxypropyl:CoM transferase
- EaCoMT
- 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)

comment:
Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.


entry: 4.4.1.24
name: --- - sulfolactate sulfo-lyase - Suy - SuyAB
sysname: 3-sulfolactate bisulfite-lyase
reaction: 3-sulfolactate = pyruvate + bisulfite
comment:
Requires iron(II). This inducible enzyme from Paracoccus pantotrophus NKNCYSA forms part of the cysteate-degradation pathway. L-Cysteate [(2S)-2-amino-3-sulfopropanoate] serves as a sole source of carbon and energy for the aerobic growth of bacteria, as an electron acceptor for several sulfate-reducing bacteria, as an electron donor for some nitrate-reducing bacteria and as a substrate for a fermentation in a sulfate-reducing baterium.


entry: 4.4.1.25
name: --- - L-cysteate sulfo-lyase - L-cysteate sulfo-lyase (deaminating) - CuyA
sysname: L-cysteate bisulfite-lyase (deaminating)
reaction: L-cysteate + H2O = pyruvate + bisulfite + NH3
comment:
A pyridoxal-phosphate protein. D-Cysteine can also act as a substrate, but more slowly. It is converted into pyruvate, sulfide and NH3. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.


entry: 4.5.1.1
name: --- - DDT-dehydrochlorinase - DDT-ase
sysname: 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase
iubmb_reaction: R04522
reaction:
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride [RN:R04522]


entry: 4.5.1.2
name: --- - 3-chloro-D-alanine dehydrochlorinase - beta-chloro-D-alanine dehydrochlorinase
sysname: 3-chloro-D-alanine chloride-lyase (deaminating)
reaction: 3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 [RN:R01031]
iubmb_reaction: R01031
comment:
A pyridoxal-phosphate protein. Also catalyses beta-replacement reactions, e.g. converts 3-chloro-D-alanine and H2S into D-cysteine and HCl.


entry: 4.5.1.4
sysname: L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating)
reaction: L-2-amino-4-chloropent-4-enoate + H2O = 2-oxopent-4-enoate + chloride + NH3 [RN:R02605]
iubmb_reaction: R02605
name:
--- 
- L-2-amino-4-chloropent-4-enoate dehydrochlorinase
- L-2-amino-4-chloro-4-pentenoate dehalogenase


entry: 4.5.1.-
name: --- []
reaction:
(1) 1,1-Dichloro-2,2-bis(4'-chlorophenyl)ethane <=> 1-Chloro-2,2-bis(4'-chlorophenyl)ethylene + HCl [RN:R05384]; (2) 1-Chloro-2,2-bis(4'-chlorophenyl)ethane <=> unsym-Bis(4'-chlorophenyl)ethylene + HCl [RN:R05385]; (3) gamma-Hexachlorocyclohexane <=> gamma-Pentachlorocyclohexene + HCl [RN:R05386]; (4) gamma-Pentachlorocyclohexene <=> 1,3,4,6-Tetrachloro-1,4-cyclohexadiene + HCl [RN:R05387]; (5) 5-Chloro-1,2,4-trihydroxybenzene <=> 2-Hydroxy-1,4-benzoquinone + HCl [RN:R05388]


entry: 4.6.1.1
name: --- - adenylate cyclase - adenylylcyclase - adenyl cyclase - 3',5'-cyclic AMP synthetase
sysname: ATP diphosphate-lyase (cyclizing)
reaction: ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
iubmb_reaction: R00089
kegg_reaction: R00434
comment:
Also acts on dATP to form 3',5'-cyclic dAMP. Requires pyruvate. Activated by NAD+ in the presence of EC 2.4.2.31 NAD(P)+-arginine ADP-ribosyltransferase .


entry: 4.6.1.3
name: --- - Transferred to 4.2.3.4
comment:
Transferred entry: now EC 4.2.3.4, 3-dehydroquinate synthase (EC 4.6.1.3 created 1978, deleted 2000)


entry: 4.6.1.4
name: --- - Transferred to 4.2.3.5
comment:
Transferred entry: now EC 4.2.3.5, chorismate synthase (EC 4.6.1.4 created 1978, modified 1983, deleted 2000)


entry: 4.6.1.8
name: --- - Transferred to 4.2.3.10
comment:
Transferred entry: now EC 4.2.3.10, (-)-endo-fenchol synthase (EC 4.6.1.8 created 1992, deleted 2000)


entry: 4.6.1.9
name: --- - Transferred to 4.2.3.11
comment:
Transferred entry: now EC 4.2.3.11, sabinene-hydrate synthase (EC 4.6.1.9 created 1992, deleted 2000)


entry: 4.6.1.10
name: --- - Transferred to 4.2.3.12
comment:
Transferred entry: now EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase (EC 4.6.1.10 created 1999, deleted 2000)


entry: 4.6.1.12
name: --- - 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase - MECDP-synthase
sysname: 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing)
iubmb_reaction: R05637
reaction:
2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP [RN:R05637]


entry: 4.6.1.13
sysname: 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
reaction: 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol [RN:R03364]
iubmb_reaction: R03364
kegg_reaction: R03332
name:
--- 
- phosphatidylinositol diacylglycerol-lyase
- monophosphatidylinositol phosphodiesterase
- phosphatidylinositol phospholipase C
- 1-phosphatidylinositol phosphodiesterase
- 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming)

comment:
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.


entry: 4.6.1.14
iubmb_reaction: (other) R04459
kegg_reaction: R04459
name:
--- 
- glycosylphosphatidylinositol diacylglycerol-lyase
- (glycosyl)phosphatidylinositol-specific phospholipase C
- GPI-PLC
- GPI-specific phospholipase C
- VSG-lipase
- glycosyl inositol phospholipid anchor-hydrolyzing enzyme
- glycosylphosphatidylinositol-phospholipase C
- glycosylphosphatidylinositol-specific phospholipase C
- variant-surface-glycoprotein phospholipase C

sysname:
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)

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 glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D.

reaction:
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol


entry: 4.6.1.15
name: --- - FAD-AMP lyase (cyclizing) - FMN cyclase
sysname: FAD AMP-lyase (cyclic-FMN-forming)
reaction: FAD = AMP + riboflavin cyclic-4',5'-phosphate
comment:
Requires Mn2+ or Co2+. While FAD was the best substrate tested [2], the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.


entry: 4.6.1.-
name: --- []
reaction:
2,3-Bisphospho-D-glycerate + ATP <=> Cyclic 2,3-bisphospho-D-glycerate + ADP + Orthophosphate [RN:R03298]


entry: 4.99.1.1
sysname: protoheme ferro-lyase
reaction: protoporphyrin + Fe2+ = protoheme + 2 H+ [RN:R00310]
iubmb_reaction: R00310
name:
--- 
- ferrochelatase
- ferro-protoporphyrin chelatase
- iron chelatase
- heme synthetase
- heme synthase


entry: 4.99.1.2
name: --- - alkylmercury lyase - organomercury lyase - organomercurial lyase
sysname: alkylmercury mercuric-lyase
reaction: RHg+ + H+ = RH + Hg2+ [RN:R03529]
iubmb_reaction: R03529
comment:
Acts on CH3Hg+ and a number of other alkylmercury and arylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide.


entry: 4.99.1.3
sysname: sirohydrochlorin cobalt-lyase
reaction: sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+ [RN:R05807]
iubmb_reaction: R05807
name:
--- 
- sirohydrochlorin cobaltochelatase
- CbiK
- CbiX
- CbiXS
- anaerobic cobalt chelatase
- cobaltochelatase [ambiguous]

comment:
This enzyme is a type II chelatase, being either a monomer (CbiX) or a homodimer (CibK) and being ATP-independent. CbiK from Salmonella enterica uses precorrin-2 as the substrate to yield cobalt-precorrin-2. The enzyme contains two histidines at the active site that are thought to be involved in the deprotonation of the tetrapyrrole substrate as well as in metal binding. CbiX from Bacillus megaterium inserts cobalt at the level of sirohydrochlorin (factor-II) rather than precorrin-2.


entry: 4.99.1.4
name: --- - sirohydrochlorin ferrochelatase - CysG - Met8P - SirB
sysname: sirohydrochlorin ferro-lyase
reaction: sirohydrochlorin + Fe2+ = siroheme + 2 H+ [RN:R02864]
iubmb_reaction: R02864
comment:
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.


entry: 4.99.1.5
name: --- - aliphatic aldoxime dehydratase - OxdA
sysname: aliphatic aldoxime hydro-lyase
reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O
comment:
The enzyme from Pseudomonas chlororaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity. The enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate. No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime.


entry: 4.99.1.6
sysname: (indol-3-yl)acetaldehyde-oxime hydro-lyase
reaction: (indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O [RN:R04093]
iubmb_reaction: R04093
kegg_reaction: R02827
name:
--- 
- indoleacetaldoxime dehydratase
- indoleacetaldoxime hydro-lyase
- 3-indoleacetaldoxime hydro-lyase
- indole-3-acetaldoxime hydro-lyase
- indole-3-acetaldehyde-oxime hydro-lyase


entry: 4.99.1.7
name: --- - phenylacetaldoxime dehydratase - PAOx dehydratase - arylacetaldoxime dehydratase - OxdB
sysname: (Z)-phenylacetaldehyde-oxime hydro-lyase
reaction: (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
comment:
The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity. (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate-heme complex, which regulates enzyme activity [2]. The enzyme is active towards several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas Fe2+ and Sn2+ have an activatory effect.


entry: 5.1.1.8
sysname: 4-hydroxyproline 2-epimerase
comment: Also interconverts trans-4-hydroxy-D-proline and cis-4-hydroxy-L-proline.
reaction: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline [RN:R03296]
iubmb_reaction: R03296
name:
--- 
- 4-hydroxyproline epimerase
- hydroxyproline epimerase
- hydroxyproline 2-epimerase
- L-hydroxyproline epimerase


entry: 5.1.1.11
sysname: phenylalanine racemase (ATP-hydrolysing)
reaction: ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine [RN:R00686]
iubmb_reaction: R00686
name:
--- 
- phenylalanine racemase (ATP-hydrolysing)
- phenylalanine racemase
- phenylalanine racemase (adenosine triphosphate-hydrolysing)
- gramicidin S synthetase I


entry: 5.1.1.15
name: --- - 2-aminohexano-6-lactam racemase - alpha-amino-epsilon-caprolactam racemase
sysname: 2-aminohexano-6-lactam racemase
reaction: L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam [RN:R04736]
iubmb_reaction: R04736
comment:
contains pyridoxal 5'-phosphate. Also racemises 2-aminopentano-5-lactam (alpha-amino-Delta-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does not catalyse the racemisation of alpha-amino acids but has some transaminase activity with them.


entry: 5.1.1.16
name: --- - protein-serine epimerase - protein-serine racemase
sysname: [protein]-serine epimerase
reaction: [protein]-L-serine = [protein]-D-serine [RN:R05175]
iubmb_reaction: R05175
comment:
the enzyme specifically interconverts the configuration of Ser-46 of the peptide omega-agatoxin-KT, found in the venom of the funnel web spider, Agelenopsis aperta, but not that of the other serine residue, Ser-28.


entry: 5.1.2.3
sysname: 3-hydroxybutanoyl-CoA 3-epimerase
reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA [RN:R03276]
iubmb_reaction: R03276
kegg_reaction: R04755
name:
--- 
- 3-hydroxybutyryl-CoA epimerase
- 3-hydroxybutyryl coenzyme A epimerase
- 3-hydroxyacyl-CoA epimerase


entry: 5.1.2.6
name: --- - isocitrate epimerase
sysname: (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate 1-epimerase
comment: (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly occurring isomer of isocitrate.
iubmb_reaction: R02318
reaction:
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate [RN:R02318]


entry: 5.1.2.-
name: --- []
reaction:
2-Hydroxy-2H-benzo[h]chromene-2-carboxylate <=> cis-4-(1'-Hydroxynaphth-2'-yl)-2-oxobut-3-enoate [RN:R05642]


entry: 5.1.3.1
sysname: D-ribulose-5-phosphate 3-epimerase
reaction: D-ribulose 5-phosphate = D-xylulose 5-phosphate [RN:R01529]
iubmb_reaction: R01529
name:
--- 
- ribulose-phosphate 3-epimerase
- phosphoribulose epimerase
- erythrose-4-phosphate isomerase
- phosphoketopentose 3-epimerase
- xylulose phosphate 3-epimerase
- phosphoketopentose epimerase
- ribulose 5-phosphate 3-epimerase
- D-ribulose phosphate-3-epimerase
- D-ribulose 5-phosphate epimerase
- D-ribulose-5-P 3-epimerase
- D-xylulose-5-phosphate 3-epimerase
- pentose-5-phosphate 3-epimerase

comment:
The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.


entry: 5.1.3.2
sysname: UDP-glucose 4-epimerase
comment: Requires NAD+. Also acts on UDP-2-deoxyglucose.
reaction: UDP-glucose = UDP-galactose [RN:R00291]
iubmb_reaction: R00291
kegg_reaction: R02984
name:
--- 
- UDP-glucose 4-epimerase
- UDP-galactose 4-epimerase
- uridine diphosphoglucose epimerase
- galactowaldenase
- UDPG-4-epimerase
- uridine diphosphate galactose 4-epimerase
- uridine diphospho-galactose-4-epimerase
- UDP-glucose epimerase
- 4-epimerase
- uridine diphosphoglucose 4-epimerase
- uridine diphosphate glucose 4-epimerase
- UDP-D-galactose 4-epimerase


entry: 5.1.3.4
sysname: L-ribulose-5-phosphate 4-epimerase
comment: Requires a divalent cation for activity.
reaction: L-ribulose 5-phosphate = D-xylulose 5-phosphate [RN:R05850]
iubmb_reaction: R05850
name:
--- 
- L-ribulose-5-phosphate 4-epimerase
- phosphoribulose isomerase
- ribulose phosphate 4-epimerase
- L-ribulose-phosphate 4-epimerase
- L-ribulose 5-phosphate 4-epimerase
- AraD
- L-Ru5P


entry: 5.1.3.5
sysname: UDP-L-arabinose 4-epimerase
reaction: UDP-L-arabinose = UDP-D-xylose [RN:R01473]
iubmb_reaction: R01473
name:
--- 
- UDP-arabinose 4-epimerase
- uridine diphosphoarabinose epimerase
- UDP arabinose epimerase
- uridine 5'-diphosphate-D-xylose 4-epimerase
- UDP-D-xylose 4-epimerase


entry: 5.1.3.6
sysname: UDP-glucuronate 4-epimerase
reaction: UDP-glucuronate = UDP-D-galacturonate [RN:R01385]
iubmb_reaction: R01385
name:
--- 
- UDP-glucuronate 4-epimerase
- uridine diphospho-D-galacturonic acid
- UDP glucuronic epimerase
- uridine diphosphoglucuronic epimerase
- UDP-galacturonate 4-epimerase
- uridine diphosphoglucuronate epimerase
- UDP-D-galacturonic acid 4-epimerase


entry: 5.1.3.7
sysname: UDP-N-acetyl-D-glucosamine 4-epimerase
reaction: UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-galactosamine [RN:R00418]
iubmb_reaction: R00418
name:
--- 
- UDP-N-acetylglucosamine 4-epimerase
- UDP acetylglucosamine epimerase
- uridine diphosphoacetylglucosamine epimerase
- uridine diphosphate N-acetylglucosamine-4-epimerase
- uridine 5'-diphospho-N-acetylglucosamine-4-epimerase


entry: 5.1.3.8
sysname: N-acyl-D-glucosamine 2-epimerase
comment: Requires catalytic amounts of ATP.
reaction: N-acyl-D-glucosamine = N-acyl-D-mannosamine [RN:R02652]
iubmb_reaction: R02652 > R01207
name:
--- 
- N-acylglucosamine 2-epimerase
- acylglucosamine 2-epimerase
- N-acetylglucosamine 2-epimerase


entry: 5.1.3.9
sysname: N-acyl-D-glucosamine-6-phosphate 2-epimerase
reaction: N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate [RN:R02770]
iubmb_reaction: R02770 > R02087
name:
--- 
- N-acylglucosamine-6-phosphate 2-epimerase
- acylglucosamine-6-phosphate 2-epimerase
- acylglucosamine phosphate 2-epimerase


entry: 5.1.3.10
sysname: CDP-3,6-dideoxy-D-glucose 2-epimerase
reaction: CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose [RN:R04266]
iubmb_reaction: R04266
name:
--- 
- CDP-paratose 2-epimerase
- CDP-paratose epimerase
- cytidine diphosphoabequose epimerase
- cytidine diphosphodideoxyglucose epimerase
- cytidine diphosphoparatose epimerase
- cytidine diphosphate paratose-2-epimerase
- CDP-abequose epimerase (incorrect)
- CDP-D-abequose 2-epimerase (incorrect)

comment:
Requires NAD+. CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more systematically called CDP-alpha-3,6-dideoxy-D-ribo-hexose. CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called CDP-3,6-dideoxy-D-arabino-hexose.


entry: 5.1.3.12
sysname: UDP-glucuronate 5'-epimerase
comment: Requires NAD+.
reaction: UDP-glucuronate = UDP-L-iduronate [RN:R01387]
iubmb_reaction: R01387
name:
--- 
- UDP-glucuronate 5'-epimerase
- uridine diphosphoglucuronate 5'-epimerase
- UDP-glucuronic acid 5'-epimerase
- C-5-uronosyl epimerase


entry: 5.1.3.13
sysname: dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase
comment: The enzyme occurs in a complex with EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase.
reaction: dTDP-4-dehydro-6-deoxy-D-glucose = dTDP-4-dehydro-6-deoxy-L-mannose [RN:R06514]
iubmb_reaction: R06514 > R02774
kegg_reaction: R02775
name:
--- 
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-L-rhamnose synthetase
- thymidine diphospho-4-ketorhamnose 3,5-epimerase
- TDP-4-ketorhamnose 3,5-epimerase
- dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase
- TDP-4-keto-L-rhamnose-3,5-epimerase


entry: 5.1.3.14
sysname: UDP-N-acetyl-D-glucosamine 2-epimerase
comment: The enzyme hydrolyses the product to UDP and N-acetyl-D-mannosamine.
reaction: UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420]
iubmb_reaction: R00420
kegg_reaction: R00414
name:
--- 
- UDP-N-acetylglucosamine 2-epimerase
- UDP-N-acetylglucosamine 2'-epimerase
- uridine diphosphoacetylglucosamine 2'-epimerase
- uridine diphospho-N-acetylglucosamine 2'-epimerase
- uridine diphosphate-N-acetylglucosamine-2'-epimerase


entry: 5.1.3.17
sysname: poly[(1,4)-beta-D-glucuronosyl-(1,4)-N-sulfo-alpha-D-glucosaminyl] glucurono-5-epimerase
reaction: heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate [RN:R04389]
iubmb_reaction: R04389
name:
--- 
- heparosan-N-sulfate-glucuronate 5-epimerase
- heparosan epimerase
- heparosan-N-sulfate-D-glucuronosyl 5-epimerase
- C-5 uronosyl epimerase
- polyglucuronate epimerase
- D-glucuronyl C-5 epimerase

comment:
Acts on D-glucuronosyl residues adjacent to sulfated D-glucosamine units in the heparin precursor. Not identical with EC 5.1.3.19 chondroitin-glucuronate 5-epimerase.


entry: 5.1.3.18
sysname: GDP-mannose 3,5-epimerase
reaction: GDP-mannose = GDP-L-galactose [RN:R00889]
iubmb_reaction: R00889
name:
--- 
- GDP-mannose 3,5-epimerase
- GDP-D-mannose:GDP-L-galactose epimerase
- guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate L-galactose epimerase


entry: 5.1.3.19
sysname: chondroitin-D-glucuronate 5-epimerase
comment: Not identical with EC 5.1.3.17 heparosan-N-sulfate-glucuronate 5-epimerase.
reaction: chondroitin D-glucuronate = dermatan L-iduronate [RN:R04104]
iubmb_reaction: R04104
name:
--- 
- chondroitin-glucuronate 5-epimerase
- polyglucuronate 5-epimerase
- dermatan-sulfate 5-epimerase
- urunosyl C-5 epimerase
- chondroitin D-glucuronosyl 5-epimerase


entry: 5.1.3.21
name: --- - maltose epimerase
sysname: maltose 1-epimerase
reaction: alpha-maltose = beta-maltose [RN:R07319]
iubmb_reaction: R07319
comment:
The enzyme catalyses the interconversion of alpha and beta anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose.


entry: 5.1.3.22
name: --- - L-ribulose-5-phosphate 3-epimerase - L-xylulose 5-phosphate 3-epimerase - UlaE - SgaU
sysname: L-ribulose-5-phosphate 3-epimerase
reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate [RN:R03244]
iubmb_reaction: R03244
comment:
Along with EC 4.1.1.85, 3-dehydro-L-gulonate-6-phosphate decarboxylase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.


entry: 5.1.99.1
sysname: methylmalonyl-CoA 2-epimerase
reaction: (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA [RN:R02765]
iubmb_reaction: R02765
name:
--- 
- methylmalonyl-CoA epimerase
- methylmalonyl-CoA racemase
- methylmalonyl coenzyme A racemase
- DL-methylmalonyl-CoA racemase
- 2-methyl-3-oxopropanoyl-CoA 2-epimerase [incorrect]


entry: 5.1.99.4
name: --- - alpha-methylacyl-CoA racemase
sysname: 2-methylacyl-CoA 2-epimerase
reaction: (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA [RN:R04729]
iubmb_reaction: R04729
comment:
alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids


entry: 5.2.1.2
sysname: 4-maleylacetoacetate cis-trans-isomerase
comment: Also acts on maleylpyruvate.
reaction: 4-maleylacetoacetate = 4-fumarylacetoacetate [RN:R03181]
iubmb_reaction: R03181
name:
--- 
- maleylacetoacetate isomerase
- maleylacetoacetic isomerase
- maleylacetone isomerase
- maleylacetone cis-trans-isomerase


entry: 5.2.1.6
name: --- - furylfuramide isomerase
sysname: 2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide cis-trans-isomerase
comment: Requires NADH.
iubmb_reaction: R04538
reaction:
(E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide = (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide [RN:R04538]


entry: 5.2.1.7
name: --- - retinol isomerase - all-trans-retinol isomerase
sysname: all-trans-retinol 11-cis-trans-isomerase
reaction: all-trans-retinol = 11-cis-retinol [RN:R02369]
iubmb_reaction: R02369
comment:
Converts all-trans-retinol to 11-cis-retinol in the dark, thus reversing the effect of EC 5.2.1.3 retinal isomerase.


entry: 5.2.1.8
sysname: peptidylproline cis-trans-isomerase
reaction: peptidylproline (omega=180) = peptidylproline (omega=0) [RN:R04273]
iubmb_reaction: R04273
name:
--- 
- peptidylprolyl isomerase
- PPIase
- cyclophilin [misleading, see comments]
- peptide bond isomerase
- peptidyl-prolyl cis-trans isomerase

comment:
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.


entry: 5.2.1.10
sysname: 2-chloro-4-carboxymethylenebut-2-en-1,4-olide cis-trans-isomerase
iubmb_reaction: R04576
name:
--- 
- 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase
- 2-chlorocarboxymethylenebutenolide isomerase
- chlorodienelactone isomerase

reaction:
cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide = trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide [RN:R04576]


entry: 5.2.1.11
name: --- - Deleted entry
comment:
Deleted entry: 4-hydroxyphenylacetaldehyde-oxime isomerase. The existence of this enzyme has been called into question by one of the authors of the reference cited (EC 5.2.1.11 created 1992, deleted 2005)


entry: 5.3.1.1
sysname: D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate [RN:R01015]
iubmb_reaction: R01015
name:
--- 
- triose-phosphate isomerase
- phosphotriose isomerase
- triose phosphoisomerase
- triose phosphate mutase
- D-glyceraldehyde-3-phosphate ketol-isomerase


entry: 5.3.1.3
sysname: D-arabinose aldose-ketose-isomerase
comment: Also acts on L-fucose and, more slowly, on L-galactose and D-altrose.
reaction: D-arabinose = D-ribulose [RN:R01577]
iubmb_reaction: R01577
name:
--- 
- arabinose isomerase
- D-arabinose(L-fucose) isomerase
- D-arabinose isomerase
- L-fucose isomerase
- D-arabinose ketol-isomerase


entry: 5.3.1.6
sysname: D-ribose-5-phosphate aldose-ketose-isomerase
comment: Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
reaction: D-ribose 5-phosphate = D-ribulose 5-phosphate [RN:R01056]
iubmb_reaction: R01056
name:
--- 
- ribose-5-phosphate isomerase
- phosphopentosisomerase
- phosphoriboisomerase
- ribose phosphate isomerase
- 5-phosphoribose isomerase
- D-ribose 5-phosphate isomerase
- D-ribose-5-phosphate ketol-isomerase


entry: 5.3.1.8
sysname: D-mannose-6-phosphate aldose-ketose-isomerase
comment: A zinc protein.
reaction: D-mannose 6-phosphate = D-fructose 6-phosphate [RN:R00772]
iubmb_reaction: R00772 > R01819
name:
--- 
- mannose-6-phosphate isomerase
- phosphomannose isomerase
- phosphohexomutase
- phosphohexoisomerase
- mannose phosphate isomerase
- phosphomannoisomerase
- D-mannose-6-phosphate ketol-isomerase


entry: 5.3.1.9
sysname: D-glucose-6-phosphate aldose-ketose-isomerase
comment: Also catalyses the anomerization of D-glucose 6-phosphate.
reaction: D-glucose 6-phosphate = D-fructose 6-phosphate [RN:R00771]
iubmb_reaction: R00771 > R02740 R03321
kegg_reaction: R02739
name:
--- 
- glucose-6-phosphate isomerase
- phosphohexose isomerase
- phosphohexomutase
- oxoisomerase
- hexosephosphate isomerase
- phosphosaccharomutase
- phosphoglucoisomerase
- phosphohexoisomerase
- phosphoglucose isomerase
- glucose phosphate isomerase
- hexose phosphate isomerase
- D-glucose-6-phosphate ketol-isomerase


entry: 5.3.1.10
name: --- - Transferred to 3.5.99.6
comment:
transferred entry: now EC 3.5.99.6 glucosamine-6-phosphate deaminase (EC 5.3.1.10 created 1961, deleted 2000)


entry: 5.3.1.12
sysname: D-glucuronate aldose-ketose-isomerase
comment: Also converts D-galacturonate to D-tagaturonate.
reaction: D-glucuronate = D-fructuronate [RN:R01482]
iubmb_reaction: R01482
kegg_reaction: R01983
name:
--- 
- glucuronate isomerase
- uronic isomerase
- uronate isomerase
- D-glucuronate isomerase
- uronic acid isomerase
- D-glucuronate ketol-isomerase


entry: 5.3.1.13
sysname: D-arabinose-5-phosphate aldose-ketose-isomerase
reaction: D-arabinose 5-phosphate = D-ribulose 5-phosphate [RN:R01530]
iubmb_reaction: R01530
name:
--- 
- arabinose-5-phosphate isomerase
- arabinose phosphate isomerase
- phosphoarabinoisomerase
- D-arabinose-5-phosphate ketol-isomerase


entry: 5.3.1.16
iubmb_reaction: R04640
name:
--- 
- 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
- N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5"-phosphoribosyl)-4- imidazolecarboxamide isomerase
- phosphoribosylformiminoaminophosphoribosylimidazolecarboxamide isomerase
- N-(phosphoribosylformimino) aminophosphoribosylimidazolecarboxamide isomerase
- 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ketol-isomerase

sysname:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imid azole-4-carboxamide aldose-ketose-isomerase

reaction:
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5- phosphoribosyl)imidazole-4-carboxamide [RN:R04640]


entry: 5.3.1.17
sysname: 4-deoxy-L-threo-5-hexosulose-uronate aldose-ketose-isomerase
reaction: 4-deoxy-L-threo-5-hexosulose uronate = 3-deoxy-D-glycero-2,5-hexodiulosonate [RN:R04383]
iubmb_reaction: R04383
name:
--- 
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
- 4-deoxy-L-threo-5-hexulose uronate isomerase


entry: 5.3.1.18
name: --- - Deleted entry
comment:
Deleted entry: glucose isomerase. Reaction is due to EC 5.3.1.9 glucose-6-phosphate isomerase, in the presence of arsenate, or EC 5.3.1.5 xylose isomerase (EC 5.3.1.18 created 1972, deleted 1978)


entry: 5.3.1.19
name: --- - Transferred to 2.6.1.16
comment:
Transferred entry: now EC 2.6.1.16 glutamine-fructose-6-phosphate aminotransferase (isomerizing) (EC 5.3.1.19 created 1972, deleted 1984)


entry: 5.3.1.23
sysname: S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase
reaction: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate [RN:R04420]
iubmb_reaction: R04420
name:
--- 
- S-methyl-5-thioribose-1-phosphate isomerase
- methylthioribose 1-phosphate isomerase
- 1-PMTR isomerase
- 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase
- S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase
- S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate aldose-ketose-isomerase
- 1-phospho-5'-S-methylthioribose isomerase
- S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase


entry: 5.3.1.24
sysname: N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase
iubmb_reaction: R03509
name:
--- 
- phosphoribosylanthranilate isomerase
- PRA isomerase
- PRAI
- IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
- N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase

comment:
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].

reaction:
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate [RN:R03509]


entry: 5.3.1.-
name: --- []
reaction:
(1) L-Xylulose <=> L-Lyxose [RN:R01906]; (2) Kanosamine 6-phosphate <=> Aminofructose 6-phosphate [RN:R06589]


entry: 5.3.3.1
sysname: 3-oxosteroid Delta5-Delta4-isomerase
comment: May be at least three distinct enzymes.
reaction: A 3-oxo-Delta5-steroid = a 3-oxo-Delta4-steroid [RN:R02644]
iubmb_reaction: R02644
name:
--- 
- steroid Delta-isomerase
- hydroxysteroid isomerase
- steroid isomerase
- Delta5-ketosteroid isomerase
- Delta5(or Delta4)-3-keto steroid isomerase
- Delta5-steroid isomerase
- 3-oxosteroid isomerase
- Delta5-3-keto steroid isomerase
- Delta5-3-oxosteroid isomerase

kegg_reaction:
R01837 R01839 R02216 R02217 R02499 R02500 R02840 R02842 R03327 R03328 R04163 R04164 R04678 R04680 R04849 R04851 R07427


entry: 5.3.3.2
sysname: isopentenyl-diphosphate Delta3-Delta2-isomerase
reaction: isopentenyl diphosphate = dimethylallyl diphosphate [RN:R01123]
iubmb_reaction: R01123
name:
--- 
- isopentenyl-diphosphate Delta-isomerase
- isopentenylpyrophosphate Delta-isomerase
- methylbutenylpyrophosphate isomerase
- isopentenylpyrophosphate isomerase

comment:
The enzyme from Streptomyces sp. strain CL190 requires FMN and NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD, but the enzyme becomes inactive when NAD(P)H is replaced by NAD+ or NADP+. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.


entry: 5.3.3.3
sysname: vinylacetyl-CoA Delta3-Delta2-isomerase
comment: Also acts on 3-methyl-vinylacetyl-CoA.
reaction: vinylacetyl-CoA = crotonyl-CoA [RN:R03031]
iubmb_reaction: R03031
name:
--- 
- vinylacetyl-CoA Delta-isomerase
- vinylacetyl coenzyme A Delta-isomerase
- vinylacetyl coenzyme A isomerase
- Delta3-cis-Delta2-trans-enoyl-CoA isomerase


entry: 5.3.3.7
name: --- - aconitate Delta-isomerase - aconitate isomerase
sysname: aconitate Delta2-Delta3-isomerase
reaction: trans-aconitate = cis-aconitate [RN:R02244]
iubmb_reaction: R02244
comment:
cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. This isomerization could take place either in a direct cis-trans interconversion or by an allelic rearrangement; the enzyme has been shown to catalyse the latter change.


entry: 5.3.3.8
sysname: dodecenoyl-CoA (3Z)-(2E)-isomerase
reaction: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA [RN:R04100]
iubmb_reaction: R04100
kegg_reaction: R04756
name:
--- 
- dodecenoyl-CoA isomerase
- dodecenoyl-CoA Delta-isomerase
- Delta3-cis-Delta2-trans-enoyl-CoA isomerase
- acetylene-allene isomerase
- dodecenoyl-CoA Delta3-cis-Delta2-trans-isomerase

comment:
Also catalyses the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C6 to C12.


entry: 5.3.3.9
name: --- - prostaglandin-A1 Delta-isomerase - prostaglandin A isomerase
sysname: (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate Delta10-Delta11-isomerase
comment: Interconverts prostaglandin A1 and prostaglandin C1.
iubmb_reaction: R04565
reaction:
(13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate = (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate [RN:R04565]


entry: 5.3.3.11
name: --- - isopiperitenone Delta-isomerase
sysname: isopiperitenone Delta8-Delta4-isomerase
reaction: isopiperitenone = piperitenone [RN:R03782]
iubmb_reaction: R03782
comment:
Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.


entry: 5.3.3.12
sysname: L-dopachrome keto-enol isomerase
reaction: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate [RN:R03673]
iubmb_reaction: R03673
name:
--- 
- L-dopachrome isomerase
- dopachrome tautomerase
- tyrosinase-related protein 2
- TRP-1
- TRP2
- TRP-2
- tyrosinase-related protein-2
- dopachrome Delta7,Delta2-isomerase
- dopachrome Delta-isomerase
- dopachrome conversion factor
- dopachrome isomerase
- dopachrome oxidoreductase
- dopachrome-rearranging enzyme
- DCF
- DCT
- dopachrome keto-enol isomerase
- L-dopachrome-methyl ester tautomerase

comment:
A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84, D-dopachrome decarboxylase).


entry: 5.3.3.13
sysname: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Delta8,11-Delta7,9-isomerase (trans-double-bond-forming)
reaction: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate [RN:R06502]
iubmb_reaction: R06502
name:
--- 
- polyenoic fatty acid isomerase
- PFI
- eicosapentaenoate cis-Delta5,8,11,14,17-eicosapentaenoate cis-Delta5-trans-Delta7,9-cis-Delta14,17 isomerase
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,8-isomerase (incorrect)
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,9-isomerase (trans-double-bond-forming)

comment:
The enzyme from the red alga Ptilota filicina catalyses the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogues, such as arachidonate and gamma-linolenate, to yield a conjugated triene.


entry: 5.3.3.14
sysname: decenoyl-[acyl-carrier-protein] Delta2-trans-Delta3-cis-isomerase
reaction: trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein]
name:
--- 
- trans-2-decenoyl-[acyl-carrier protein] isomerase
- beta-hydroxydecanoyl thioester dehydrase
- trans-2-cis-3-decenoyl-ACP isomerase
- trans-2,cis-3-decenoyl-ACP isomerase
- trans-2-decenoyl-ACP isomerase
- FabM

comment:
While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.


entry: 5.3.3.-
name: --- []
reaction:
(1) 2-Hydroxymuconate <=> (Z)-5-Oxohex-2-enedioate [RN:R03966]; (2) 2-Oxohept-3-enedioate <=> 2-Hydroxyhepta-2,4-dienedioate [RN:R04134]


entry: 5.3.4.1
name: --- - protein disulfide-isomerase - S-S rearrangase
sysname: protein disulfide-isomerase
reaction: Catalyses the rearrangement of -S-S- bonds in proteins
comment:
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.


entry: 5.3.99.1
name: --- - Deleted entry
comment:
Deleted entry: hydroperoxide isomerase. Reaction due to combined action of EC 4.2.1.92 (hydroperoxide dehydratase) and EC 5.3.99.6 (allene-oxide cyclase) (EC 5.3.99.1 created 1972, deleted 1992)


entry: 5.3.99.2
sysname: (5,13)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase
comment: Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
iubmb_reaction: R02266
name:
--- 
- prostaglandin-D synthase
- prostaglandin-H2 D-isomerase
- prostaglandin-R-prostaglandin D isomerase
- PGH-PGD isomerase

reaction:
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate [RN:R02266]


entry: 5.3.99.3
sysname: (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat e E-isomerase
comment: Brings about the opening of the epidioxy bridge. Requires glutathione.
iubmb_reaction: R02265
name:
--- 
- prostaglandin-E synthase
- prostaglandin-H2 E-isomerase
- endoperoxide isomerase
- prostaglandin R-prostaglandin E isomerase
- prostaglandin endoperoxide E isomerase
- PGE isomerase
- PGH-PGE isomerase
- PGE2 isomerase
- prostaglandin endoperoxide E2 isomerase
- prostaglandin H-E isomerase

reaction:
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265]


entry: 5.3.99.4
sysname: (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat e 6-isomerase
comment: Converts prostaglandin H2 into prostaglandin I2 (prostacyclin). A heme-thiolate protein.
iubmb_reaction: R02267
name:
--- 
- prostaglandin-I synthase
- prostacyclin synthase
- prostacycline synthetase
- prostagladin I2 synthetase
- PGI2 synthase
- PGI2 synthetase

reaction:
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- dienoate [RN:R02267]


entry: 5.3.99.5
sysname: (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoat e isomerase
comment: Converts prostaglandin H2 into thromboxane A2. A heme-thiolate protein.
iubmb_reaction: R02268
name:
--- 
- thromboxane-A synthase
- thromboxane synthase
- (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate thromboxane-A2-isomerase

reaction:
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13- dienoate [RN:R02268]


entry: 5.3.99.6
name: --- - allene-oxide cyclase
sysname: (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate isomerase (cyclizing)
reaction: (9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate [RN:R03402]
iubmb_reaction: R03402
comment:
Allene oxides formed by the action of EC 4.2.1.92 hydroperoxide dehydratase, are converted into cyclopentenone derivatives.


entry: 5.3.99.8
sysname: violaxanthin-capsorubin isomerase (ketone-forming)
reaction: (1) violaxanthin = capsorubin [RN:R07320]; (2) antheraxanthin = capsanthin [RN:R07321]
iubmb_reaction: R07320 R07321
name:
--- 
- capsanthin/capsorubin synthase
- CCS
- ketoxanthophyll synthase
- capsanthin-capsorubin synthase

comment:
This multifunctional enzyme is induced during chromoplast differentiation in plants [1]. Isomerization of the epoxide ring of violaxanthin gives the cyclopentyl-ketone of capsorubin or capsanthin.


entry: 5.3.99.9
name: --- - neoxanthin synthase - NSY
sysname: violaxanthin-neoxanthin isomerase (epoxide-opening)
reaction: violaxanthin = neoxanthin [RN:R06948]
iubmb_reaction: R06948
comment:
The opening of the epoxide ring of violaxanthin generates a chiral allene. Neoxanthin is a precursor of the plant hormone abscisic acid and the last product of carotenoid synthesis in green plants [2].


entry: 5.3.99.-
name: --- []
reaction:
(1) trans-O-Hydroxybenzylidenepyruvate <=> 2-Hydroxychromene-2-carboxylate [RN:R05137]; (2) 2-Hydroxy-8-methylchromene-2-carboxylate <=> 2-Hydroxy-3-methylbenzalpyruvate [RN:R06912]; (3) 2-Carboxy-2-hydroxy-8-carboxychromene <=> 2-Hydroxy-3-carboxybenzalpyruvate [RN:R06922]; (4) 2-Hydroxy-7-hydroxymethylchromene-2-carboxylate <=> 2-Hydroxy-4-hydroxymethylbenzalpyruvate [RN:R06933]


entry: 5.4.2.1
sysname: D-phosphoglycerate 2,3-phosphomutase
reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate [RN:R01518]
iubmb_reaction: R01518
kegg_reaction: R01662
name:
--- 
- phosphoglycerate mutase
- phosphoglycerate phosphomutase
- phosphoglyceromutase
- glycerate phosphomutase (diphosphoglycerate cofactor)
- monophosphoglycerate mutase
- monophosphoglyceromutase
- diphosphoglycomutase
- diphosphoglycerate mutase
- bisphosphoglyceromutase
- GriP mutase
- MPGM
- PGA mutase
- PGAM-i
- PGAM
- PGAM-d
- PGM

comment:
The enzymes from mammals and from yeast are phosphorylated by (2R)-2,3-bis-phosphoglycerate, which is also an intermediate (see introduction to section EC 5.4.2). With the rabbit muscle enzyme, dissociation of bisphosphate from the enzyme is much slower than the overall isomerization. These enzymes also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase; they were formerly listed as EC 2.7.5.3. Enzymes from wheat, rice, insects and some fungi, however, have maximum activity in the absence of 2,3-bisphosphoglycerate, and were formerly listed under the present number as phosphoglycerate phosphomutase.


entry: 5.4.2.2
name: --- - phosphoglucomutase - glucose phosphomutase - phosphoglucose mutase
sysname: alpha-D-glucose 1,6-phosphomutase
reaction: alpha-D-glucose 1-phosphate = D-glucose 6-phosphate [RN:R00959]
iubmb_reaction: R00959
kegg_reaction: R01057 R02299 R03319
comment:
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate.


entry: 5.4.2.3
sysname: N-acetyl-alpha-D-glucosamine 1,6-phosphomutase
comment: The enzyme is activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate. Formerly EC 2.7.5.2.
reaction: N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate [RN:R02086]
iubmb_reaction: R02086
name:
--- 
- phosphoacetylglucosamine mutase
- acetylglucosamine phosphomutase
- acetylaminodeoxyglucose phosphomutase
- phospho-N-acetylglucosamine mutase
- N-acetyl-D-glucosamine 1,6-phosphomutase


entry: 5.4.2.4
sysname: 3-phospho-D-glycerate 1,2-phosphomutase
reaction: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate [RN:R01662]
iubmb_reaction: R01662
kegg_reaction: R01516 R01518
name:
--- 
- bisphosphoglycerate mutase
- diphosphoglycerate mutase
- glycerate phosphomutase
- bisphosphoglycerate synthase
- bisphosphoglyceromutase
- biphosphoglycerate synthase
- diphosphoglyceric mutase
- 2,3-diphosphoglycerate mutase
- phosphoglyceromutase
- 2,3-diphosphoglycerate synthase
- DPGM
- 2,3-bisphosphoglycerate mutase
- BPGM
- diphosphoglyceromutase
- 2,3-diphosphoglyceromutase

comment:
In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reactions of EC 3.1.3.13 (bisphosphoglycerate phosphatase) and EC 5.4.2.1 (phosphoglycerate mutase). Formerly EC 2.7.5.4.


entry: 5.4.2.5
sysname: alpha-D-glucose 1,6-phosphomutase (glucose-cofactor)
reaction: alpha-D-glucose 1-phosphate = D-glucose 6-phosphate [RN:R00959]
iubmb_reaction: R00959
name:
--- 
- phosphoglucomutase (glucose-cofactor)
- glucose phosphomutase
- glucose-1-phosphate phosphotransferase

comment:
The enzyme is activated by D-glucose, which probably acts as an acceptor for a phosphate residue from the substrate, thus being itself converted into the product.


entry: 5.4.2.7
sysname: alpha-D-ribose 1,5-phosphomutase
reaction: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate [RN:R01057]
iubmb_reaction: R01057
kegg_reaction: R02749
name:
--- 
- phosphopentomutase
- phosphodeoxyribomutase
- deoxyribose phosphomutase
- deoxyribomutase
- phosphoribomutase
- alpha-D-glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase
- D-ribose 1,5-phosphomutase

comment:
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor. Formerly EC 2.7.5.6.


entry: 5.4.2.8
sysname: alpha-D-mannose 1,6-phosphomutase
reaction: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate [RN:R01818]
iubmb_reaction: R01818
name:
--- 
- phosphomannomutase
- mannose phosphomutase
- phosphomannose mutase
- D-mannose 1,6-phosphomutase

comment:
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. Formerly EC 2.7.5.7.


entry: 5.4.2.9
sysname: phosphoenolpyruvate 2,3-phosphonomutase
reaction: phosphoenolpyruvate = 3-phosphonopyruvate [RN:R00661]
iubmb_reaction: R00661
name:
--- 
- phosphoenolpyruvate mutase
- phosphoenolpyruvate-phosphonopyruvate phosphomutase
- PEP phosphomutase
- phosphoenolpyruvate phosphomutase
- PEPPM

comment:
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.


entry: 5.4.2.10
name: --- - phosphoglucosamine mutase - D-glucosamine 1,6-phosphomutase
sysname: alpha-D-glucosamine 1,6-phosphomutase
reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate [RN:R02060]
iubmb_reaction: R02060
comment:
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of alpha-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.


entry: 5.4.3.1
name: --- - Deleted entry
comment:
Deleted entry: ornithine 4,5-aminomutase. This reaction was due to a mixture of EC 5.1.1.12 (ornithine racemase) and EC 5.4.3.5 (D-ornithine 4,5-aminomutase) (EC 5.4.3.1 created 1972, deleted 1976)


entry: 5.4.3.4
sysname: D-2,6-diaminohexanoate 5,6-aminomutase
comment: Requires a cobamide coenzyme.
reaction: D-lysine = 2,5-diaminohexanoate [RN:R02852]
iubmb_reaction: R02852
name:
--- 
- D-lysine 5,6-aminomutase
- D-alpha-lysine mutase
- adenosylcobalamin-dependent D-lysine 5,6-aminomutase


entry: 5.4.4.1
sysname: (hydroxyamino)benzene hydroxymutase
reaction: (hydroxyamino)benzene = 2-aminophenol [RN:R05383]
iubmb_reaction: R05383
name:
--- 
- (hydroxyamino)benzene mutase
- HAB mutase
- hydroxylaminobenzene hydroxymutase
- hydroxylaminobenzene mutase


entry: 5.4.99.1
sysname: L-threo-3-methylaspartate carboxy-aminomethylmutase
comment: Requires a cobamide coenzyme.
reaction: L-threo-3-methylaspartate = L-glutamate [RN:R00262]
iubmb_reaction: R00262
name:
--- 
- methylaspartate mutase
- glutamate mutase
- glutamic mutase
- glutamic isomerase
- glutamic acid mutase
- glutamic acid isomerase
- methylaspartic acid mutase
- beta-methylaspartate-glutamate mutase
- glutamate isomerase


entry: 5.4.99.2
sysname: (R)-methylmalonyl-CoA CoA-carbonylmutase
comment: Requires a cobamide coenzyme.
reaction: (R)-methylmalonyl-CoA = succinyl-CoA [RN:R00833]
iubmb_reaction: R00833
name:
--- 
- methylmalonyl-CoA mutase
- methylmalonyl-CoA CoA-carbonyl mutase
- methylmalonyl coenzyme A mutase
- methylmalonyl coenzyme A carbonylmutase
- (S)-methylmalonyl-CoA mutase
- (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]


entry: 5.4.99.3
name: --- - 2-acetolactate mutase - acetolactate mutase - acetohydroxy acid isomerase
sysname: 2-acetolactate methylmutase
reaction: 2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate [RN:R03052]
iubmb_reaction: R03052 > R05071
kegg_reaction: R05069
comment:
Requires ascorbic acid; also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate.


entry: 5.4.99.7
sysname: (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming)
reaction: (S)-2,3-epoxysqualene = lanosterol [RN:R03199]
iubmb_reaction: R03199
name:
--- 
- lanosterol synthase
- 2,3-epoxysqualene lanosterol cyclase
- squalene-2,3-oxide-lanosterol cyclase
- lanosterol 2,3-oxidosqualene cyclase
- squalene 2,3-epoxide:lanosterol cyclase
- 2,3-oxidosqualene sterol cyclase
- oxidosqualene cyclase
- 2,3-oxidosqualene cyclase
- 2,3-oxidosqualene-lanosterol cyclase
- oxidosqualene-lanosterol cyclase
- squalene epoxidase-cyclase


entry: 5.4.99.8
sysname: (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming)
reaction: (S)-2,3-epoxysqualene = cycloartenol [RN:R03200]
iubmb_reaction: R03200
name:
--- 
- cycloartenol synthase
- 2,3-epoxysqualene cycloartenol-cyclase
- squalene-2,3-epoxide-cycloartenol cyclase
- 2,3-epoxysqualene-cycloartenol cyclase
- 2,3-oxidosqualene-cycloartenol cyclase


entry: 5.4.99.10
name: --- - Deleted entry
comment:
Deleted entry: Now included with EC 5.4.99.11 isomaltulose synthase (EC 5.4.99.10 created 1984, deleted 1992)


entry: 5.4.99.11
sysname: sucrose glucosylmutase
reaction: sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose [RN:R00810 R06217]
iubmb_reaction: R00810 R06217(G)
name:
--- 
- isomaltulose synthase
- isomaltulose synthetase
- sucrose alpha-glucosyltransferase
- trehalulose synthase

comment:
The enzyme simultaneously produces isomaltulose (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from sucrose.


entry: 5.4.99.12
sysname: tRNA-uridine uracilmutase
reaction: tRNA uridine = tRNA pseudouridine [RN:R03020]
iubmb_reaction: R03020
name:
--- 
- tRNA-pseudouridine synthase I
- tRNA-uridine isomerase
- tRNA pseudouridylate synthase I
- transfer ribonucleate pseudouridine synthetase
- pseudouridine synthase
- transfer RNA pseudouridine synthetase

comment:
The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine.


entry: 5.4.99.14
sysname: 4-carboxymethyl-4-methylbut-2-en-1,4-olide methylmutase
reaction: 4-carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide [RN:R04510]
iubmb_reaction: R04510
name:
--- 
- 4-carboxymethyl-4-methylbutenolide mutase
- 4-methyl-2-enelactone isomerase
- 4-methylmuconolactone methylisomerase
- 4-methyl-3-enelactone methyl isomerase


entry: 5.4.99.15
sysname: (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
iubmb_reaction: R01824 R06243(G)
name:
--- 
- (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
- malto-oligosyltrehalose synthase
- maltodextrin alpha-D-glucosyltransferase

comment:
the enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units. Not active towards maltose.

reaction:
4-{(1->4)-alpha-D-glucosyl}(n-1)-D-glucose = 1-alpha-D-{(1->4)-alpha-D-glucosyl}(n-1)-alpha-D-glucopyranoside [RN:R01824 R06243]


entry: 5.4.99.18
sysname: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase
iubmb_reaction: R07405
name:
--- 
- 5-(carboxyamino)imidazole ribonucleotide mutase
- N5-CAIR mutase
- PurE
- N5-carboxyaminoimidazole ribonucleotide mutase

comment:
In Escherichia coli, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. In the absence of EC 6.3.2.6, phosphoribosylaminoimidazolesuccinocarboxamide synthase, the reaction is reversible [3]. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation [3].

reaction:
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [RN:R07405]


entry: 5.5.1.1
sysname: 2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
reaction: 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate [RN:R03959]
iubmb_reaction: R03959 > R06989
kegg_reaction: R04489 R05300 R05390
name:
--- 
- muconate cycloisomerase
- muconate cycloisomerase I
- cis,cis-muconate-lactonizing enzyme
- cis,cis-muconate cycloisomerase
- muconate lactonizing enzyme
- 4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing)

comment:
Requires Mn2+. Also acts (in the reverse reaction) on 3-methyl-cis,cis-hexadienedioate and, very slowly, on cis,trans-hexadienedioate. Not identical with EC 5.5.1.7 (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).


entry: 5.5.1.2
sysname: 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
reaction: 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate [RN:R03307]
iubmb_reaction: R03307
name:
--- 
- 3-carboxy-cis,cis-muconate cycloisomerase
- beta-carboxymuconate lactonizing enzyme
- 3-carboxymuconolactone hydrolase


entry: 5.5.1.4
sysname: 1D-myo-inositol-3-phosphate lyase (isomerizing)
reaction: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate [RN:R07324]
iubmb_reaction: R07324
kegg_reaction: R00840
name:
--- 
- inositol-3-phosphate synthase
- myo-inositol-1-phosphate synthase
- D-glucose 6-phosphate cycloaldolase
- inositol 1-phosphate synthatase
- glucose 6-phosphate cyclase
- inositol 1-phosphate synthetase
- glucose-6-phosphate inositol monophosphate cycloaldolase
- glucocycloaldolase
- 1L-myo-inositol-1-phosphate lyase (isomerizing)

comment:
Requires NAD+, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH reconverts C-5 into the -CHOH- form.


entry: 5.5.1.7
name: --- - chloromuconate cycloisomerase - muconate cycloisomerase II
sysname: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
reaction: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate [RN:R04259]
iubmb_reaction: R04259
kegg_reaction: R05391 R05392 R06834 R06840
comment:
Requires Mn2+. The product of cycloisomerization of 3-chloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylenebut-2-en-4-olide. Also acts (in the reverse direction) on 2-chloro-cis,cis-muconate. Not identical with EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).


entry: 5.5.1.8
sysname: (+)-bornyl-diphosphate lyase (decyclizing)
reaction: geranyl diphosphate = (+)-bornyl diphosphate [RN:R02007]
iubmb_reaction: R02007
name:
--- 
- bornyl diphosphate synthase
- bornyl pyrophosphate synthase
- bornyl pyrophosphate synthetase
- (+)-bornylpyrophosphate cyclase
- geranyl-diphosphate cyclase (ambiguous)


entry: 5.5.1.9
name: --- - cycloeucalenol cycloisomerase - cycloeucalenol-obtusifoliol isomerase
sysname: cycloeucalenol lyase (cyclopropane-decyclizing)
reaction: cycloeucalenol = obtusifoliol [RN:R03775]
iubmb_reaction: R03775
comment:
Opens the cyclopropane ring of a number of related 4alpha-methyl-9beta-19-cyclosterols, but not those with a 4beta-methyl group, with formation of an 8(9) double bond. Involved in the synthesis of plant sterols.


entry: 5.5.1.11
name: --- - dichloromuconate cycloisomerase
sysname: 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
reaction: 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate = 2,4-dichloro-cis,cis-muconate [RN:R04345]
iubmb_reaction: R04345
kegg_reaction: R05393
comment:
Requires Mn2+. The product of cyclisomerization of dichloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide. Also acts, in the reverse direction, on cis,cis-muconate and its monochloro-derivatives, but with lower affinity. Not identical with EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.7 (chloromuconate cycloisomerase).


entry: 5.5.1.12
name: --- - copalyl diphosphate synthase
sysname: (+)-copalyl-diphosphate lyase (decyclizing)
reaction: geranylgeranyl diphosphate = (+)-copalyl diphosphate [RN:R06298]
iubmb_reaction: R06298
comment:
Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 4.2.3.18 (abietadiene synthase)


entry: 5.5.1.13
name: --- - ent-copalyl diphosphate synthase - ent-kaurene synthase A - ent-kaurene synthetase A
sysname: ent-copalyl-diphosphate lyase (decyclizing)
reaction: geranylgeranyl diphosphate = ent-copalyl diphosphate [RN:R02068]
iubmb_reaction: R02068
comment:
Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)


entry: 5.99.1.2
sysname: DNA topoisomerase
reaction: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining
name:
--- 
- DNA topoisomerase
- type I DNA topoisomerase
- untwisting enzyme
- relaxing enzyme
- nicking-closing enzyme
- swivelase
- omega-protein
- deoxyribonucleate topoisomerase
- topoisomerase

comment:
These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.99.1.3 DNA topoisomerase (ATP-hydrolysing).


entry: 5.99.1.3
sysname: DNA topoisomerase (ATP-hydrolysing)
reaction: ATP-dependent breakage, passage and rejoining of double-stranded DNA
name:
--- 
- DNA topoisomerase (ATP-hydrolysing)
- type II DNA topoisomerase
- DNA-gyrase
- deoxyribonucleate topoisomerase
- deoxyribonucleic topoisomerase
- topoisomerase
- DNA topoisomerase II

comment:
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.99.1.2 DNA topoisomerase).


entry: 5.-.-.-
name: --- []
reaction:
(1) L-Ribulose 5-phosphate <=> L-Xylulose 5-phosphate [RN:R03244]; (2) D-arabino-3-Hexulose 6-phosphate <=> D-Fructose 6-phosphate [RN:R05339]; (3) Sedoheptulose 7-phosphate <=> D-glycero-D-manno-Heptose 7-phosphate [RN:R05645]


entry: 6.1.1.1
sysname: L-tyrosine:tRNA(Tyr) ligase (AMP-forming)
reaction: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr) [RN:R02918]
iubmb_reaction: R02918
name:
--- 
- tyrosine-tRNA ligase
- tyrosyl-tRNA synthetase
- L-tyrosine-tRNA(Tyr) ligase (AMP-forming)
- tyrosyl-transfer ribonucleate synthetase
- tyrosyl-transfer RNA synthetase
- tyrosyl-transfer ribonucleic acid synthetase
- tyrosyl-tRNA ligase
- tyrosine-transfer RNA ligase
- tyrosine-transfer ribonucleate synthetase
- tyrosine translase
- tyrosine tRNA synthetase


entry: 6.1.1.2
sysname: L-tryptophan:tRNA(Trp) ligase (AMP-forming)
reaction: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp) [RN:R03664]
iubmb_reaction: R03664
name:
--- 
- tryptophan-tRNA ligase
- tryptophanyl-tRNA synthetase
- L-tryptophan-tRNA(Trp) ligase (AMP-forming)
- tryptophanyl-transfer ribonucleate synthetase
- tryptophanyl-transfer ribonucleic acid synthetase
- tryptophanyl-transfer RNA synthetase
- tryptophanyl ribonucleic synthetase
- tryptophanyl-transfer ribonucleic synthetase
- tryptophanyl-tRNA synthase
- tryptophan translase
- TrpRS


entry: 6.1.1.3
sysname: L-threonine:tRNA(Thr) ligase (AMP-forming)
reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) [RN:R03663]
iubmb_reaction: R03663
name:
--- 
- threonine-tRNA ligase
- threonyl-tRNA synthetase
- threonyl-transfer ribonucleate synthetase
- threonyl-transfer RNA synthetase
- threonyl-transfer ribonucleic acid synthetase
- threonyl ribonucleic synthetase
- threonine-transfer ribonucleate synthetase
- threonine translase
- TRS


entry: 6.1.1.4
sysname: L-leucine:tRNA(Leu) ligase (AMP-forming)
reaction: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) [RN:R03657]
iubmb_reaction: R03657
name:
--- 
- leucine-tRNA ligase
- leucyl-tRNA synthetase
- leucyl-transfer ribonucleate synthetase
- leucyl-transfer RNA synthetase
- leucyl-transfer ribonucleic acid synthetase
- leucine-tRNA synthetase
- leucine translase


entry: 6.1.1.5
sysname: L-isoleucine:tRNA(Ile) ligase (AMP-forming)
reaction: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) [RN:R03656]
iubmb_reaction: R03656
name:
--- 
- isoleucine-tRNA ligase
- isoleucyl-tRNA synthetase
- isoleucyl-transfer ribonucleate synthetase
- isoleucyl-transfer RNA synthetase
- isoleucine-transfer RNA ligase
- isoleucine-tRNA synthetase
- isoleucine translase


entry: 6.1.1.6
sysname: L-lysine:tRNA(Lys) ligase (AMP-forming)
reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) [RN:R03658]
iubmb_reaction: R03658
name:
--- 
- lysine-tRNA ligase
- lysyl-tRNA synthetase
- lysyl-transfer ribonucleate synthetase
- lysyl-transfer RNA synthetase
- L-lysine-transfer RNA ligase
- lysine-tRNA synthetase
- lysine translase


entry: 6.1.1.7
sysname: L-alanine:tRNA(Ala) ligase (AMP-forming)
reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala) [RN:R03038]
iubmb_reaction: R03038
name:
--- 
- alanine-tRNA ligase
- alanyl-tRNA synthetase
- alanyl-transfer ribonucleate synthetase
- alanyl-transfer RNA synthetase
- alanyl-transfer ribonucleic acid synthetase
- alanine-transfer RNA ligase
- alanine transfer RNA synthetase
- alanine tRNA synthetase
- alanine translase
- alanyl-transfer ribonucleate synthase
- AlaRS
- Ala-tRNA synthetase


entry: 6.1.1.9
sysname: L-valine:tRNA(Val) ligase (AMP-forming)
reaction: ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val) [RN:R03665]
iubmb_reaction: R03665
name:
--- 
- valine-tRNA ligase
- valyl-tRNA synthetase
- valyl-transfer ribonucleate synthetase
- valyl-transfer RNA synthetase
- valyl-transfer ribonucleic acid synthetase
- valine transfer ribonucleate ligase
- valine translase


entry: 6.1.1.10
sysname: L-methionine:tRNA(Met) ligase (AMP-forming)
reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) [RN:R03659]
iubmb_reaction: R03659
kegg_reaction: R04773
name:
--- 
- methionine-tRNA ligase
- methionyl-tRNA synthetase
- methionyl-transfer ribonucleic acid synthetase
- methionyl-transfer ribonucleate synthetase
- methionyl-transfer RNA synthetase
- methionine translase
- MetRS

comment:
In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyses the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.


entry: 6.1.1.11
sysname: L-serine:tRNA(Ser) ligase (AMP-forming)
reaction: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser) [RN:R03662]
iubmb_reaction: R03662
name:
--- 
- serine-tRNA ligase
- seryl-tRNA synthetase
- SerRS
- seryl-transfer ribonucleate synthetase
- seryl-transfer RNA synthetase
- seryl-transfer ribonucleic acid synthetase
- serine translase

comment:
This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1, L-seryl-tRNA(Sec) selenium transferase.


entry: 6.1.1.12
sysname: L-aspartate:tRNA(Asp) ligase (AMP-forming)
reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp) [RN:R05577]
iubmb_reaction: R05577
name:
--- 
- aspartate-tRNA ligase
- aspartyl-tRNA synthetase
- aspartyl ribonucleic synthetase
- aspartyl-transfer RNA synthetase
- aspartic acid translase
- aspartyl-transfer ribonucleic acid synthetase
- aspartyl ribonucleate synthetase


entry: 6.1.1.13
sysname: D-alanine:poly(phosphoribitol) ligase (AMP-forming)
iubmb_reaction: R02718
name:
--- 
- D-alanine-poly(phosphoribitol) ligase
- D-alanyl-poly(phosphoribitol) synthetase
- "D-alanine: membrane acceptor ligase"
- D-alanine-D-alanyl carrier protein ligase
- D-alanine-membrane acceptor ligase
- D-alanine-activating enzyme

comment:
A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine. Involved in the synthesis of teichoic acids.

reaction:
ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate) [RN:R02718]


entry: 6.1.1.14
sysname: glycine:tRNA(Gly) ligase (AMP-forming)
reaction: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) [RN:R03654]
iubmb_reaction: R03654
name:
--- 
- glycine-tRNA ligase
- glycyl-tRNA synthetase
- glycyl-transfer ribonucleate synthetase
- glycyl-transfer RNA synthetase
- glycyl-transfer ribonucleic acid synthetase
- glycyl translase


entry: 6.1.1.15
sysname: L-proline:tRNA(Pro) ligase (AMP-forming)
reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) [RN:R03661]
iubmb_reaction: R03661
name:
--- 
- proline-tRNA ligase
- prolyl-tRNA synthetase
- prolyl-transferRNA synthetase
- prolyl-transfer ribonucleate synthetase
- proline translase
- prolyl-transfer ribonucleic acid synthetase
- prolyl-s-RNA synthetase
- prolinyl-tRNA ligase


entry: 6.1.1.16
sysname: L-cysteine:tRNA(Cys) ligase (AMP-forming)
reaction: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys) [RN:R03650]
iubmb_reaction: R03650
name:
--- 
- cysteine-tRNA ligase
- cysteinyl-tRNA synthetase
- cysteinyl-transferRNA synthetase
- cysteinyl-transfer ribonucleate synthetase
- cysteine translase


entry: 6.1.1.17
sysname: L-glutamate:tRNA(Glu) ligase (AMP-forming)
reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu) [RN:R05578]
iubmb_reaction: R05578
name:
--- 
- glutamate-tRNA ligase
- glutamyl-tRNA synthetase
- glutamyl-transfer ribonucleate synthetase
- glutamyl-transfer RNA synthetase
- glutamyl-transfer ribonucleic acid synthetase
- glutamate-tRNA synthetase
- glutamic acid translase


entry: 6.1.1.18
sysname: L-glutamine:tRNA(Gln) ligase (AMP-forming)
reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln) [RN:R03652]
iubmb_reaction: R03652
name:
--- 
- glutamine-tRNA ligase
- glutaminyl-tRNA synthetase
- glutaminyl-transfer RNA synthetase
- glutaminyl-transfer ribonucleate synthetase
- glutamine-tRNA synthetase
- glutamine translase
- glutamate-tRNA ligase
- glutaminyl ribonucleic acid
- GlnRS


entry: 6.1.1.19
sysname: L-arginine:tRNA(Arg) ligase (AMP-forming)
reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg) [RN:R03646]
iubmb_reaction: R03646
name:
--- 
- arginine-tRNA ligase
- arginyl-tRNA synthetase
- arginyl-transfer ribonucleate synthetase
- arginyl-transfer RNA synthetase
- arginyl transfer ribonucleic acid synthetase
- arginine-tRNA synthetase
- arginine translase


entry: 6.1.1.20
sysname: L-phenylalanine:tRNA(Phe) ligase (AMP-forming)
reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe) [RN:R03660]
iubmb_reaction: R03660
name:
--- 
- phenylalanine-tRNA ligase
- phenylalanyl-tRNA synthetase
- phenylalanyl-transfer ribonucleate synthetase
- phenylalanine-tRNA synthetase
- phenylalanyl-transfer RNA synthetase
- phenylalanyl-tRNA ligase
- phenylalanyl-transfer RNA ligase
- L-phenylalanyl-tRNA synthetase
- phenylalanine translase


