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Displaying entries 101-122 of 122.
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EC | 3.1.1.101 | ||||||||||||||||
Accepted name: | poly(ethylene terephthalate) hydrolase | ||||||||||||||||
Reaction: | (ethylene terephthalate)n + H2O = (ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate | ||||||||||||||||
Glossary: | poly(ethylene terephthalate) = PET 4-[(2-hydroxyethoxy)carbonyl]benzoate = mono(ethylene terephthalate) = MHET |
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Other name(s): | PETase; PET hydrolase | ||||||||||||||||
Systematic name: | poly(ethylene terephthalate) hydrolase | ||||||||||||||||
Comments: | The enzyme, isolated from the bacterium Ideonella sakaiensis, also produces small amounts of terephthalate (cf. EC 3.1.1.102, mono(ethylene terephthalate) hydrolase). The reaction takes place on PET-film placed in solution. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.102 | ||||||||||||||||
Accepted name: | mono(ethylene terephthalate) hydrolase | ||||||||||||||||
Reaction: | 4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = terephthalate + ethylene glycol | ||||||||||||||||
Glossary: | 4-[(2-hydroxyethoxy)carbonyl]benzoate = mono(ethylene terephthalate) = MHET |
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Other name(s): | MHET hydrolase; MHETase | ||||||||||||||||
Systematic name: | 4-[(2-hydroxyethoxy)carbonyl]benzoate acylhydrolase | ||||||||||||||||
Comments: | The enzyme, isolated from the bacterium Ideonella sakaiensis, has no activity with poly(ethylene terephthalate) PET (cf. EC 3.1.1.101, poly(ethylene terephthalate) hydrolase). | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.103 | ||||||||||||||||
Accepted name: | teichoic acid D-alanine hydrolase | ||||||||||||||||
Reaction: | [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n D-alanine | ||||||||||||||||
Glossary: | Rib-ol = ribitol | ||||||||||||||||
Other name(s): | fmtA (gene name) | ||||||||||||||||
Systematic name: | teichoic acid D-alanylhydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.104 | ||||||||||||||||
Accepted name: | 5-phospho-D-xylono-1,4-lactonase | ||||||||||||||||
Reaction: | (1) D-xylono-1,4-lactone 5-phosphate + H2O = 5-phospho-D-xylonate (2) L-arabino-1,4-lactone 5-phosphate + H2O = 5-phospho-L-arabinate |
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Systematic name: | 5-phospho-D-xylono-1,4-lactone hydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from Mycoplasma spp., contains a binuclear metal center with two zinc cations. The enzyme is specific for the phosphorylated forms, and is unable to hydrolyse non-phosphorylated 1,4-lactones. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.105 | ||||||||||||||||
Accepted name: | 3-O-acetylpapaveroxine carboxylesterase | ||||||||||||||||
Reaction: | 3-O-acetylpapaveroxine + H2O = narcotine hemiacetal + acetate | ||||||||||||||||
For diagram of noscapine biosynthesis, click here | |||||||||||||||||
Glossary: | 3-O-acetylpapaveroxine = 6-{(S)-acetoxy[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]methyl}-2,3-dimethoxybenzaldehyde narcotine hemiacetal = (3S)-6,7-dimethoxy-3-[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]-1,3-dihydroisobenzofuran-1-ol |
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Other name(s): | CXE1 (gene name) | ||||||||||||||||
Systematic name: | 3-O-acetylpapaveroxine acetatehydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.106 | ||||||||||||||||
Accepted name: | O-acetyl-ADP-ribose deacetylase | ||||||||||||||||
Reaction: | (1) 3′′-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate (2) 2′′-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate |
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Other name(s): | ymdB (gene name); MACROD1 (gene name) | ||||||||||||||||
Systematic name: | O-acetyl-ADP-D-ribose carboxylesterase | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2′′ or 3′′ position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286, protein acetyllysine N-acetyltransferase. The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.107 | ||||||||||||||||
Accepted name: | apo-salmochelin esterase | ||||||||||||||||
Reaction: | (1) enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer (2) triglucosyl-enterobactin + H2O = triglucosyl-(2,3-dihydroxybenzoylserine)3 (3) diglucosyl-enterobactin + H2O = diglucosyl-(2,3-dihydroxybenzoylserine)3 (4) monoglucosyl-enterobactin + H2O = monoglucosyl-(2,3-dihydroxybenzoylserine)3 |
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For diagram of glucosyl enterobactin biosynthesis, click here | |||||||||||||||||
Glossary: | N-(2,3-dihydroxybenzoyl)-L-serine trimer = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(2,3-dihydroxybenzoyl)-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine diglucosyl-(2,3-dihydroxybenzoylserine)3 = salmochelin S2 = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl]-N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-3→1(3)-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = salmochelin S4 = di-C-glucosyl-enterobactin triglucosyl-enterobactin = N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = tri-C-glucosyl-enterobactin = salmochelin TGE |
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Other name(s): | iroE (gene name) | ||||||||||||||||
Systematic name: | apo-salmochelin esterase | ||||||||||||||||
Comments: | This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. Unlike EC 3.1.1.108, iron(III)-enterobactin esterase, which acts only on enterobactin, this enzyme can also act on the C-glucosylated forms known as salmochelins. Unlike EC 3.1.1.109, iron(III)-salmochelin esterase (IroD), IroE prefers apo siderophores as substrates, and is assumed to act before the siderophores are exported out of the cell. It hydrolyses the trilactone only once, producing linearized trimers. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.108 | ||||||||||||||||
Accepted name: | iron(III)-enterobactin esterase | ||||||||||||||||
Reaction: | iron(III)-enterobactin + 3 H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine complex + 2 N-(2,3-dihydroxybenzoyl)-L-serine (overall reaction) (1a) iron(III)-enterobactin + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine trimer complex (1b) iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine trimer complex + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine dimer complex + N-(2,3-dihydroxybenzoyl)-L-serine (1c) iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine dimer complex + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine complex + N-(2,3-dihydroxybenzoyl)-L-serine |
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Other name(s): | fes (gene name); pfeE (gene name); enterochelin hydrolase; enterochelin esterase; ferric enterobactin esterase | ||||||||||||||||
Systematic name: | iron(III)-enterobactin hydrolase | ||||||||||||||||
Comments: | The enzyme, isolated from the bacterium Escherichia coli, allows the bacterium to grow in limited iron conditions. It can also act on enterobactin (with no complexed iron) and the aluminium(III) analogue of iron(III)-enterobactin. The trimer formed is further hydrolysed to form the dimer and the monomer. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.109 | ||||||||||||||||
Accepted name: | iron(III)-salmochelin esterase | ||||||||||||||||
Reaction: | (1) iron(III)-[diglucosyl-enterobactin] complex + H2O = iron(III)-[salmochelin S2] complex (2) iron(III)-[monoglucosyl-enterobactin] complex + H2O = iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)3] complex (3) iron(III)-[salmochelin S2] complex + H2O = iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)2] complex + N-(2,3-dihydroxybenzoyl)-L-serine (4) iron(III)-[salmochelin S2] complex + H2O = iron(III)-[salmochelin S1] complex + salmochelin SX (5) iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)3] complex + H2O = iron(III)-[salmochelin S1] complex + N-(2,3-dihydroxybenzoyl)-L-serine (6) iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)2] complex + H2O = iron(III)-[salmochelin SX] complex + salmochelin SX |
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Glossary: | salmochelin S2 = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl]-N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine salmochelin S1 = O-3-[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = salmochelin S4 = di-C-glucosyl-enterobactin salmochelin SX = N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine |
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Other name(s): | iroD (gene name); ferric-salmochelin esterase | ||||||||||||||||
Systematic name: | iron(III)-salmochelin complex hydrolase | ||||||||||||||||
Comments: | This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. The enzyme acts on iron(III)-bound enterobactin and C-glucosylated derivatives known as salmochelins. Unlike EC 3.1.1.107, apo-salmochelin esterase (IroE), IroD prefers iron(III)-bound siderophores as substrates, and is assumed to act after the iron-siderophore complexes are imported into the cell. It catalyses several hydrolytic reactions, producing a mixture of iron(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] complex and salmochelin SX. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.110 | ||||||||||||||||
Accepted name: | xylono-1,5-lactonase | ||||||||||||||||
Reaction: | D-xylono-1,5-lactone + H2O = D-xylonate | ||||||||||||||||
Other name(s): | xylC (gene name); D-xylono-1,5-lactone lactonase | ||||||||||||||||
Systematic name: | D-xylono-1,5-lactone lactonohydrolase | ||||||||||||||||
Comments: | The enzyme, found in bacteria, participates in the degradation of D-xylose. cf. EC 3.1.1.68, xylono-1,4-lactonase. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.111 | ||||||||||||||||
Accepted name: | phosphatidylserine sn-1 acylhydrolase | ||||||||||||||||
Reaction: | (1) a phosphatidylserine + H2O = a 2-acyl-1-lyso-phosphatidylserine + a fatty acid (2) a 1-acyl-2-lyso-phosphatidylserine + H2O = glycerophosphoserine + a fatty acid |
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Glossary: | phosphatidylserine = 3-sn-phosphatidyl-L-serine = 1,2-diacyl-sn-glycero-3-phospho-L-serine glycerophosphoserine = sn-glycero-3-phospho-L-serine |
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Other name(s): | phosphatidylserine-specific phospholipase A1; PS-PLA1; PLA1A (gene name) | ||||||||||||||||
Systematic name: | 3-sn-phosphatidyl-L-serine sn-1 acylhydrolase | ||||||||||||||||
Comments: | The enzyme, which has been described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.112 | ||||||||||||||||
Accepted name: | isoamyl acetate esterase | ||||||||||||||||
Reaction: | 3-methylbutyl acetate + H2O = 3-methylbutanol + acetate | ||||||||||||||||
Other name(s): | IAH1 (gene name) | ||||||||||||||||
Systematic name: | 3-methylbutyl acetate acetohydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from the yeast Saccharomyces cerevisiae, hydrolyses acetate esters. It acts preferentially on 3-methylbutyl acetate, a major determinant of sake flavor. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.113 | ||||||||||||||||
Accepted name: | ethyl acetate hydrolase | ||||||||||||||||
Reaction: | ethyl acetate + H2O = acetate + ethanol | ||||||||||||||||
Other name(s): | mekB (gene name); estZ (gene name) | ||||||||||||||||
Systematic name: | ethyl acetate acetohydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from Pseudomonas strains, is involved in degradation of short chain alkyl methyl ketones. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.114 | ||||||||||||||||
Accepted name: | methyl acetate hydrolase | ||||||||||||||||
Reaction: | methyl acetate + H2O = acetate + methanol | ||||||||||||||||
Other name(s): | acmB (gene name) | ||||||||||||||||
Systematic name: | methyl acetate acetohydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Gordonia sp. TY-5, participates in a propane utilization pathway. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.115 | ||||||||||||||||
Accepted name: | D-apionolactonase | ||||||||||||||||
Reaction: | D-apionolactone + H2O = D-apionate | ||||||||||||||||
Glossary: | D-apionolactone = (3R,4R)-3,4-dihydroxy-4-(hydroxymethyl)oxolan-2-one | ||||||||||||||||
Other name(s): | apnL (gene name) | ||||||||||||||||
Systematic name: | D-apionolactone lactonohydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.116 | ||||||||||||||||
Accepted name: | sn-1-specific diacylglycerol lipase | ||||||||||||||||
Reaction: | a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid | ||||||||||||||||
Other name(s): | DAGLA (gene name); DAGLB (gene name) | ||||||||||||||||
Systematic name: | diacylglycerol sn-1-acylhydrolase | ||||||||||||||||
Comments: | The enzyme, present in animals, is specific for the sn-1 position. When acting on 1-acyl-2-arachidonoyl-sn-glycerol, the enzyme forms 2-arachidonoylglycerol, the most abundant endocannabinoid in the mammalian brain. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.117 | ||||||||||||||||
Accepted name: | (4-O-methyl)-D-glucuronate—lignin esterase | ||||||||||||||||
Reaction: | a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol | ||||||||||||||||
Other name(s): | glucuronoyl esterase (ambiguous); 4-O-methyl-glucuronoyl methylesterase; glucuronoyl-lignin ester hydrolase | ||||||||||||||||
Systematic name: | (4-O-methyl)-D-glucuronate—lignin ester hydrolase | ||||||||||||||||
Comments: | The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 3.1.1.118 | ||||||||||||||||
Accepted name: | phospholipid sn-1 acylhydrolase | ||||||||||||||||
Reaction: | (1) a 1-phosphatidyl-1D-myo-inositol + H2O = a 2-acyl-sn-glycero-3-phospho-1D-myo-inositol + a fatty acid (2) a 1,2-diacyl-sn-glycerol 3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid |
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Glossary: | a 1,2-diacyl-sn-glycerol 3-phosphate = a phosphatidate | ||||||||||||||||
Other name(s): | phospholipase DDHD1; phosphatidic acid-preferring phospholipase A1; PA-PLA1; DDHD1 (gene name) | ||||||||||||||||
Systematic name: | phospholipid sn-1 acylhydrolase | ||||||||||||||||
Comments: | The human enzyme shows broad specificity, and has a preference for phosphatidate over other phospholipids. Unlike EC 3.1.1.32, phospholipase A1, it is also active against phosphatidylinositol. It is not active towards acyl groups linked at the sn-2 position. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.119 | ||||||||||||||||
Transferred entry: | exo-acting protein-α-N-acetylgalactosaminidase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 3.2.1.217, exo-acting protein-α-N-acetylgalactosaminidase. | ||||||||||||||||
EC | 3.1.1.120 | ||||||||||||||||
Accepted name: | L-fucono-1,5-lactonase | ||||||||||||||||
Reaction: | L-fucono-1,5-lactone + H2O = L-fuconate | ||||||||||||||||
For diagram of L-fucose catabolism, click here | |||||||||||||||||
Systematic name: | L-fucono-1,5-lactone lactonohydrolase | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Burkholderia multivorans, participates in an L-fucose degradation pathway. The enzyme exhibits catalytic activity for the hydrolysis of several lactones, including L-fucono-1,4-lactone, D-arabinono-1,4-lactone, L-xylono-1,4-lactone, and L-galactono-1,4-lactone, but L-fucono-1,5-lactone is the best substrate. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.121 | ||||||||||||||||
Accepted name: | ergosteryl-3β-O-L-aspartate hydrolase | ||||||||||||||||
Reaction: | 1-(ergostan-3β-yl) L-aspartate + H2O = ergosterol + L-aspartate | ||||||||||||||||
Other name(s): | ErdH | ||||||||||||||||
Systematic name: | ergosteryl-3β-O-L-aspartate aminoacylesterase | ||||||||||||||||
Comments: | The enzyme has been detected in fungal species that belong to the Ascomycota and Basidiomycota phyla, and has been characterized from the fungus Aspergillus fumigatus. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||
References: |
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EC | 3.1.1.122 | ||||||||||||||||
Accepted name: | carbendazim hydrolysing esterase | ||||||||||||||||
Reaction: | carbendazim + H2O = 2-aminobenzimidazole + CO2 + methanol (overall reaction) (1a) carbendazim + H2O = N-(1H-1,3-benzodiazol-2-yl)carbamate + methanol (1b) N-(1H-1,3-benzodiazol-2-yl)carbamate = 2-aminobenzimidazole + CO2 (spontaneous) |
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Glossary: | carbendazim = methyl 1H-benzimidazol-2-ylcarbamate; 2-aminobenzimidazole = 1H-benzimidazol-2-amine | ||||||||||||||||
Other name(s): | mheI (gene name) | ||||||||||||||||
Systematic name: | carbendazim methanol hydrolase (decarboxylating) | ||||||||||||||||
Comments: | The enzyme, which is inducible in the soil bacterium Nocardioides sp. (strain SG-4G), catalyses the degradation of the fungicide carbendazim. Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 10605-21-7 | ||||||||||||||||
References: |
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