The Enzyme Database

Displaying entries 101-150 of 530.

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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
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
References:
1.  Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., Toyohara, K., Miyamoto, K., Kimura, Y. and Oda, K. A bacterium that degrades and assimilates poly(ethylene terephthalate). Science 351 (2016) 1196–1199. [DOI] [PMID: 26965627]
[EC 3.1.1.101 created 2016]
 
 
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
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
References:
1.  Yoshida, S., Hiraga, K., Takehana, T., Taniguchi, I., Yamaji, H., Maeda, Y., Toyohara, K., Miyamoto, K., Kimura, Y. and Oda, K. A bacterium that degrades and assimilates poly(ethylene terephthalate). Science 351 (2016) 1196–1199. [DOI] [PMID: 26965627]
[EC 3.1.1.102 created 2016]
 
 
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
References:
1.  Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C.Y. and Suginaka, H. Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 2355–2361. [PMID: 9371333]
2.  Qamar, A. and Golemi-Kotra, D. Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob. Agents Chemother. 56 (2012) 3797–3805. [DOI] [PMID: 22564846]
3.  Rahman, M.M., Hunter, H.N., Prova, S., Verma, V., Qamar, A. and Golemi-Kotra, D. The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids. MBio 7 (2016) e02070. [DOI] [PMID: 26861022]
[EC 3.1.1.103 created 2018]
 
 
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
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
References:
1.  Korczynska, M., Xiang, D.F., Zhang, Z., Xu, C., Narindoshvili, T., Kamat, S.S., Williams, H.J., Chang, S.S., Kolb, P., Hillerich, B., Sauder, J.M., Burley, S.K., Almo, S.C., Swaminathan, S., Shoichet, B.K. and Raushel, F.M. Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry 53 (2014) 4727–4738. [PMID: 24955762]
[EC 3.1.1.104 created 2018]
 
 
EC 3.1.1.105     
Accepted name: 3-O-acetylpapaveroxine carboxylesterase
Reaction: 3-O-acetylpapaveroxine + H2O = narcotine hemiacetal + acetate
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
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:
1.  Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104–106. [PMID: 25485687]
2.  Park, M.R., Chen, X., Lang, D.E., Ng, K.KS. and Facchini, P.J. Heterodimeric O-methyltransferases involved in the biosynthesis of noscapine in opium poppy. Plant J. 95 (2018) 252–267. [PMID: 29723437]
[EC 3.1.1.105 created 2019]
 
 
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
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
References:
1.  Chen, D., Vollmar, M., Rossi, M.N., Phillips, C., Kraehenbuehl, R., Slade, D., Mehrotra, P.V., von Delft, F., Crosthwaite, S.K., Gileadi, O., Denu, J.M. and Ahel, I. Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J. Biol. Chem. 286 (2011) 13261–13271. [PMID: 21257746]
2.  Zhang, W., Wang, C., Song, Y., Shao, C., Zhang, X. and Zang, J. Structural insights into the mechanism of Escherichia coli YmdB: A 2′-O-acetyl-ADP-ribose deacetylase. J. Struct. Biol. 192 (2015) 478–486. [PMID: 26481419]
3.  Agnew, T., Munnur, D., Crawford, K., Palazzo, L., Mikoc, A. and Ahel, I. MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria. Front. Microbiol. 9:20 (2018). [PMID: 29410655]
[EC 3.1.1.106 created 2019]
 
 
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
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
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, ferric 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, ferric 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:
1.  Lin, H., Fischbach, M.A., Liu, D.R. and Walsh, C.T. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 127 (2005) 11075–11084. [PMID: 16076215]
[EC 3.1.1.107 created 2019]
 
 
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
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
References:
1.  O'Brien, I.G., Cox, G.B. and Gibson, F. Enterochelin hydrolysis and iron metabolism in Escherichia coli. Biochim. Biophys. Acta 237 (1971) 537–549. [PMID: 4330269]
2.  Greenwood, K.T. and Luke, R.K. Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia Coli K-12. Properties of enterochelin esterase. Biochim. Biophys. Acta 525 (1978) 209–218. [PMID: 150859]
3.  Pettis, G.S. and McIntosh, M.A. Molecular characterization of the Escherichia coli enterobactin cistron entF and coupled expression of entF and the fes gene. J. Bacteriol. 169 (1987) 4154–4162. [PMID: 3040679]
4.  Brickman, T.J. and McIntosh, M.A. Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J. Biol. Chem. 267 (1992) 12350–12355. [PMID: 1534808]
5.  Winkelmann, G., Cansier, A., Beck, W. and Jung, G. HPLC separation of enterobactin and linear 2,3-dihydroxybenzoylserine derivatives: a study on mutants of Escherichia coli defective in regulation (fur), esterase (fes) and transport (fepA). Biometals 7 (1994) 149–154. [PMID: 8148617]
6.  Perraud, Q., Moynie, L., Gasser, V., Munier, M., Godet, J., Hoegy, F., Mely, Y., Mislin, G.LA., Naismith, J.H. and Schalk, I.J. A key role for the periplasmic PfeE esterase in iron acquisition via the siderophore enterobactin in Pseudomonas aeruginosa. ACS Chem. Biol. 13 (2018) 2603–2614. [PMID: 30086222]
[EC 3.1.1.108 created 2019]
 
 
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
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
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:
1.  Lin, H., Fischbach, M.A., Liu, D.R. and Walsh, C.T. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 127 (2005) 11075–11084. [PMID: 16076215]
[EC 3.1.1.109 created 2019]
 
 
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:
1.  Toivari, M., Nygard, Y., Kumpula, E.P., Vehkomaki, M.L., Bencina, M., Valkonen, M., Maaheimo, H., Andberg, M., Koivula, A., Ruohonen, L., Penttila, M. and Wiebe, M.G. Metabolic engineering of Saccharomyces cerevisiae for bioconversion of D-xylose to D-xylonate. Metab. Eng. 14 (2012) 427–436. [PMID: 22709678]
2.  Nygard, Y., Maaheimo, H., Mojzita, D., Toivari, M., Wiebe, M., Resnekov, O., Gustavo Pesce, C., Ruohonen, L. and Penttila, M. Single cell and in vivo analyses elucidate the effect of xylC lactonase during production of D-xylonate in Saccharomyces cerevisiae. Metab. Eng. 25 (2014) 238–247. [PMID: 25073011]
[EC 3.1.1.110 created 2019]
 
 
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
Glossary: phosphatidylserine = 3-sn-phosphatidyl-L-serine = 1,2-diacyl-sn-glycero-3-phospho-L-serine
glycerophosphoserine = sn-glycero-3-phospho-L-serine
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:
1.  Sato, T., Aoki, J., Nagai, Y., Dohmae, N., Takio, K., Doi, T., Arai, H. and Inoue, K. Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family. J. Biol. Chem. 272 (1997) 2192–2198. [PMID: 8999922]
2.  Nagai, Y., Aoki, J., Sato, T., Amano, K., Matsuda, Y., Arai, H. and Inoue, K. An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J. Biol. Chem. 274 (1999) 11053–11059. [PMID: 10196188]
3.  Hosono, H., Aoki, J., Nagai, Y., Bandoh, K., Ishida, M., Taguchi, R., Arai, H. and Inoue, K. Phosphatidylserine-specific phospholipase A1 stimulates histamine release from rat peritoneal mast cells through production of 2-acyl-1-lysophosphatidylserine. J. Biol. Chem. 276 (2001) 29664–29670. [PMID: 11395520]
4.  Aoki, J., Nagai, Y., Hosono, H., Inoue, K. and Arai, H. Structure and function of phosphatidylserine-specific phospholipase A1. Biochim. Biophys. Acta 1582 (2002) 26–32. [PMID: 12069807]
[EC 3.1.1.111 created 2019]
 
 
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
References:
1.  Fukuda, K., Kiyokawa, Y., Yanagiuchi, T., Wakai, Y., Kitamoto, K., Inoue, Y. and Kimura, A. Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli. Appl. Microbiol. Biotechnol. 53 (2000) 596–600. [PMID: 10855721]
[EC 3.1.1.112 created 2019]
 
 
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:
1.  Hasona, A., York, S.W., Yomano, L.P., Ingram, L.O. and Shanmugam, K.T. Decreasing the level of ethyl acetate in ethanolic fermentation broths of Escherichia coli KO11 by expression of Pseudomonas putida estZ esterase. Appl. Environ. Microbiol. 68 (2002) 2651–2659. [PMID: 12039716]
2.  Onaca, C., Kieninger, M., Engesser, K.H. and Altenbuchner, J. Degradation of alkyl methyl ketones by Pseudomonas veronii MEK700. J. Bacteriol. 189 (2007) 3759–3767. [PMID: 17351032]
[EC 3.1.1.113 created 2019]
 
 
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:
1.  Kotani, T., Yurimoto, H., Kato, N. and Sakai, Y. Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp. strain TY-5. J. Bacteriol. 189 (2007) 886–893. [DOI] [PMID: 17071761]
[EC 3.1.1.114 created 2019]
 
 
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:
1.  Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696–705. [DOI] [PMID: 29867142]
[EC 3.1.1.115 created 2020]
 
 
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:
1.  Chau, L.Y. and Tau, H.H. Release of arachidonate from diglyceride in human platelets requires the sequential action of a diglyceride lipase and a monoglyceride lipase. Biochem. Biophys. Res. Commun. 100 (1988) 1688–1695. [DOI] [PMID: 7295321]
2.  Bisogno, T., Howell, F., Williams, G., Minassi, A., Cascio, M.G., Ligresti, A., Matias, I., Schiano-Moriello, A., Paul, P., Williams, E.J., Gangadharan, U., Hobbs, C., Di Marzo, V. and Doherty, P. Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J. Cell Biol. 163 (2003) 463–468. [DOI] [PMID: 14610053]
3.  Bisogno, T. Assay of DAGLα/β activity. Methods Mol. Biol. 1412 (2016) 149–156. [DOI] [PMID: 27245901]
[EC 3.1.1.116 created 2021]
 
 
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
References:
1.  Spanikova, S. and Biely, P. Glucuronoyl esterase--novel carbohydrate esterase produced by Schizophyllum commune. FEBS Lett. 580 (2006) 4597–4601. [DOI] [PMID: 16876163]
2.  Charavgi, M.D., Dimarogona, M., Topakas, E., Christakopoulos, P. and Chrysina, E.D. The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 63–73. [DOI] [PMID: 23275164]
3.  Arnling Baath, J., Giummarella, N., Klaubauf, S., Lawoko, M. and Olsson, L. A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-carbohydrate ester bonds. FEBS Lett. 590 (2016) 2611–2618. [DOI] [PMID: 27397104]
4.  Huttner, S., Klaubauf, S., de Vries, R.P. and Olsson, L. Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds. Appl. Microbiol. Biotechnol. 101 (2017) 5301–5311. [DOI] [PMID: 28429057]
5.  Huynh, H.H. and Arioka, M. Functional expression and characterization of a glucuronoyl esterase from the fungus Neurospora crassa: identification of novel consensus sequences containing the catalytic triad. J. Gen. Appl. Microbiol. 62 (2016) 217–224. [DOI] [PMID: 27600355]
6.  Arnling Baath, J., Mazurkewich, S., Knudsen, R.M., Poulsen, J.N., Olsson, L., Lo Leggio, L. and Larsbrink, J. Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion. Biotechnol Biofuels 11:213 (2018). [DOI] [PMID: 30083226]
7.  Mazurkewich, S., Poulsen, J.N., Lo Leggio, L. and Larsbrink, J. Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components. J. Biol. Chem. 294 (2019) 19978–19987. [DOI] [PMID: 31740581]
8.  Ernst, H.A., Mosbech, C., Langkilde, A.E., Westh, P., Meyer, A.S., Agger, J.W. and Larsen, S. The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nat. Commun. 11:1026 (2020). [DOI] [PMID: 32094331]
[EC 3.1.1.117 created 2021]
 
 
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
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:
1.  Yamashita, A., Kumazawa, T., Koga, H., Suzuki, N., Oka, S. and Sugiura, T. Generation of lysophosphatidylinositol by DDHD domain containing 1 (DDHD1): Possible involvement of phospholipase D/phosphatidic acid in the activation of DDHD1. Biochim. Biophys. Acta 1801 (2010) 711–720. [DOI] [PMID: 20359546]
2.  Baba, T., Kashiwagi, Y., Arimitsu, N., Kogure, T., Edo, A., Maruyama, T., Nakao, K., Nakanishi, H., Kinoshita, M., Frohman, M.A., Yamamoto, A. and Tani, K. Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics. J. Biol. Chem. 289 (2014) 11497–11511. [DOI] [PMID: 24599962]
[EC 3.1.1.118 created 2021]
 
 
EC 3.1.2.1     
Accepted name: acetyl-CoA hydrolase
Reaction: acetyl-CoA + H2O = CoA + acetate
Other name(s): acetyl-CoA deacylase; acetyl-CoA acylase; acetyl coenzyme A hydrolase; acetyl coenzyme A deacylase; acetyl coenzyme A acylase; acetyl-CoA thiol esterase
Systematic name: acetyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-54-7
References:
1.  Gergely, J., Hele, P. and Ramakrishnan, C.V. Succinyl and acetyl coenzyme A deacylases. J. Biol. Chem. 198 (1952) 323–334. [PMID: 12999747]
[EC 3.1.2.1 created 1961]
 
 
EC 3.1.2.2     
Accepted name: palmitoyl-CoA hydrolase
Reaction: palmitoyl-CoA + H2O = CoA + palmitate
Other name(s): long-chain fatty-acyl-CoA hydrolase; palmitoyl coenzyme A hydrolase; palmitoyl thioesterase; palmitoyl coenzyme A hydrolase; palmitoyl-CoA deacylase; palmityl thioesterase; palmityl-CoA deacylase; fatty acyl thioesterase I; palmityl thioesterase I
Systematic name: palmitoyl-CoA hydrolase
Comments: Also hydrolyses CoA thioesters of other long-chain fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-87-0
References:
1.  Barnes, E.M., Jr. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J. Biol. Chem. 243 (1968) 2955–2962. [PMID: 4871199]
2.  Berge, R.K. and Farstad, M. Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria. Methods Enzymol. 71 (1981) 234–242. [PMID: 6116156]
3.  Miyazawa, S., Furuta, S. and Hashimoto, T. Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators. Eur. J. Biochem. 117 (1981) 425–430. [DOI] [PMID: 6115749]
4.  Srere, P.A., Seubert, W. and Lynen, F. Palmityl coenzyme A deacylase. Biochim. Biophys. Acta 33 (1959) 313–319. [DOI] [PMID: 13670899]
5.  Yabusaki, K.K. and Ballou, C.E. Long-chain fatty acyl-CoA thioesterases from Mycobacterium smegmatis. Methods Enzymol. 71 (1981) 242–246.
[EC 3.1.2.2 created 1961]
 
 
EC 3.1.2.3     
Accepted name: succinyl-CoA hydrolase
Reaction: succinyl-CoA + H2O = CoA + succinate
Other name(s): succinyl-CoA acylase; succinyl coenzyme A hydrolase; succinyl coenzyme A deacylase
Systematic name: succinyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-86-9
References:
1.  Gergely, J., Hele, P. and Ramakrishnan, C.V. Succinyl and acetyl coenzyme A deacylases. J. Biol. Chem. 198 (1952) 323–334. [PMID: 12999747]
[EC 3.1.2.3 created 1961]
 
 
EC 3.1.2.4     
Accepted name: 3-hydroxyisobutyryl-CoA hydrolase
Reaction: 3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate
Other name(s): 3-hydroxy-isobutyryl CoA hydrolase; HIB CoA deacylase
Systematic name: 3-hydroxy-2-methylpropanoyl-CoA hydrolase
Comments: Also hydrolyses 3-hydroxypropanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-88-1
References:
1.  Rendina, G. and Coon, M.J. Enzymatic hydrolysis of the coenzyme A thiol esters of β-hydroxypropionic and β-hydroxyisobutyric acids. J. Biol. Chem. 225 (1957) 523–534. [PMID: 13457352]
[EC 3.1.2.4 created 1961]
 
 
EC 3.1.2.5     
Accepted name: hydroxymethylglutaryl-CoA hydrolase
Reaction: (S)-3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate
For diagram of the mevalonate-biosynthesis pathway, click here
Other name(s): β-hydroxy-β-methylglutaryl coenzyme A hydrolase; β-hydroxy-β-methylglutaryl coenzyme A deacylase; hydroxymethylglutaryl coenzyme A hydrolase; hydroxymethylglutaryl coenzyme A deacylase; 3-hydroxy-3-methylglutaryl-CoA hydrolase
Systematic name: (S)-3-hydroxy-3-methylglutaryl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-89-2
References:
1.  Dekker, E.E., Schlesinger, M.J. and Coon, M.J. β-Hydroxy-β-methylglutaryl coenzyme A deacetylase. J. Biol. Chem. 233 (1958) 434–438. [PMID: 13563516]
[EC 3.1.2.5 created 1961]
 
 
EC 3.1.2.6     
Accepted name: hydroxyacylglutathione hydrolase
Reaction: S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
Other name(s): glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase
Systematic name: S-(2-hydroxyacyl)glutathione hydrolase
Comments: Also hydrolyses S-acetoacetylglutathione, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-90-5
References:
1.  Racker, E. Spectrophotometric measurements of the metabolic formation and degradation of thiol esters and enediol compounds. Biochim. Biophys. Acta 9 (1952) 577–579. [DOI] [PMID: 13032160]
2.  Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938–3943. [PMID: 4200890]
3.  Uotila, L. Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12 (1973) 3944–3951. [PMID: 4745654]
[EC 3.1.2.6 created 1961 (EC 3.1.2.8 created 1961, incorporated 1978)]
 
 
EC 3.1.2.7     
Accepted name: glutathione thiolesterase
Reaction: S-acylglutathione + H2O = glutathione + a carboxylate
Other name(s): citryl-glutathione thioesterhydrolase
Systematic name: S-acylglutathione hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-99-4
References:
1.  Kielley, W.W. and Bradley, L.B. Glutathione thiolesterase. J. Biol. Chem. 206 (1954) 327–338. [PMID: 13130552]
[EC 3.1.2.7 created 1961]
 
 
EC 3.1.2.8      
Deleted entry:  S-acetoacylglutathione hydrolase. Now included with EC 3.1.2.6 hydroxyacylglutathione hydrolase
[EC 3.1.2.8 created 1961, deleted 1978]
 
 
EC 3.1.2.9      
Deleted entry:  S-acetoacetylhydrolipoate hydrolase
[EC 3.1.2.9 created 1961, deleted 1964]
 
 
EC 3.1.2.10     
Accepted name: formyl-CoA hydrolase
Reaction: formyl-CoA + H2O = CoA + formate
Other name(s): formyl coenzyme A hydrolase
Systematic name: formyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-91-6
References:
1.  Sly, W.S. and Stadtman, E.R. Formate metabolism. I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl phosphate in Clostridium kluyveri. J. Biol. Chem. 238 (1963) 2632–2638. [PMID: 14063284]
[EC 3.1.2.10 created 1965]
 
 
EC 3.1.2.11     
Accepted name: acetoacetyl-CoA hydrolase
Reaction: acetoacetyl-CoA + H2O = CoA + acetoacetate
For diagram of mevalonate biosynthesis, click here
Other name(s): acetoacetyl coenzyme A hydrolase; acetoacetyl CoA deacylase; acetoacetyl coenzyme A deacylase
Systematic name: acetoacetyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-10-1
References:
1.  Aragón, J.J. and Lowenstein, J.M. A survey of enzymes which generate or use acetoacetyl thioesters in rat liver. J. Biol. Chem. 258 (1983) 4725–4733. [PMID: 6131897]
2.  Drummond, G.I. and Stern, J.R. Enzymes of ketone body metabolism. II. Properties of an acetoacetate-synthesizing enzyme prepared from ox liver. J. Biol. Chem. 235 (1960) 318–325. [PMID: 13818236]
[EC 3.1.2.11 created 1972]
 
 
EC 3.1.2.12     
Accepted name: S-formylglutathione hydrolase
Reaction: S-formylglutathione + H2O = glutathione + formate
Systematic name: S-formylglutathione hydrolase
Comments: Also hydrolyses S-acetylglutathione, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 83380-83-0
References:
1.  Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938–3943. [PMID: 4200890]
2.  Uotila, L. and Koivusalo, M. Purification and properties of S-formylglutathione hydrolase from human liver. J. Biol. Chem. 249 (1974) 7664–7672. [PMID: 4436331]
3.  Harms, N., Ras, J., Reijnders, W.N., van Spanning, R.J. and Stouthamer, A.H. S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? J. Bacteriol. 178 (1996) 6296–6299. [DOI] [PMID: 8892832]
[EC 3.1.2.12 created 1978]
 
 
EC 3.1.2.13     
Accepted name: S-succinylglutathione hydrolase
Reaction: S-succinylglutathione + H2O = glutathione + succinate
Systematic name: S-succinylglutathione hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 50812-22-1
References:
1.  Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938–3943. [PMID: 4200890]
2.  Uotila, L. Purification and properties of S-succinylglutathione hydrolase from human liver. J. Biol. Chem. 254 (1979) 7024–7029. [PMID: 457667]
[EC 3.1.2.13 created 1978]
 
 
EC 3.1.2.14     
Accepted name: oleoyl-[acyl-carrier-protein] hydrolase
Reaction: an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate
Other name(s): acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase; oleoyl-[acyl-carrier-protein] hydrolase
Systematic name: oleoyl-[acyl-carrier protein] hydrolase
Comments: Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68009-83-6
References:
1.  Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382–391. [DOI] [PMID: 30409]
2.  Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins. Arch. Biochem. Biophys. 172 (1976) 110–116. [DOI] [PMID: 3134]
[EC 3.1.2.14 created 1984]
 
 
EC 3.1.2.15      
Deleted entry: This activity is covered by EC 3.4.19.12, ubiquitinyl hydrolase 1
[EC 3.1.2.15 created 1986, deleted 2014]
 
 
EC 3.1.2.16     
Accepted name: citrate-lyase deacetylase
Reaction: acetyl-[citrate (pro-3S)-lyase] + H2O = holo-[citrate (pro-3S)-lyase] + acetate
Other name(s): [citrate-(pro-3S)-lyase] thiolesterase; acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase; citrate lyase deacetylase; [citrate-(pro-3S)-lyase](acetyl-form) hydrolase
Systematic name: acetyl-[citrate-(pro-3S)-lyase] hydrolase
Comments: In the proteobacterium Rubrivivax gelatinosus, this enzyme modulates the activity of EC 4.1.3.6, citrate (pro-3S)-lyase, by converting it from its active acetyl form into its inactive thiol form by removal of its acetyl groups [2]. The activity of citrate-lyase deacetylase is itself inhibited by L-glutamate [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58319-93-0
References:
1.  Giffhorn, F. and Gottschalk, G. Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+)-glutamate. J. Bacteriol. 124 (1975) 1052–1061. [PMID: 356]
2.  Giffhorn, F., Rode, H., Kuhn, A. and Gottschalk, G. Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate. Eur. J. Biochem. 111 (1980) 461–471. [DOI] [PMID: 7460909]
[EC 3.1.2.16 created 1989]
 
 
EC 3.1.2.17     
Accepted name: (S)-methylmalonyl-CoA hydrolase
Reaction: (S)-methylmalonyl-CoA + H2O = methylmalonate + CoA
Other name(s): D-methylmalonyl-coenzyme A hydrolase
Systematic name: (S)-methylmalonyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87928-03-8
References:
1.  Kovachy, R.J., Copley, S.D. and Allen, R.H. Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase. J. Biol. Chem. 258 (1983) 11415–11421. [PMID: 6885824]
[EC 3.1.2.17 created 1989]
 
 
EC 3.1.2.18     
Accepted name: ADP-dependent short-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): short-chain acyl coenzyme A hydrolase; propionyl coenzyme A hydrolase; propionyl-CoA hydrolase; propionyl-CoA thioesterase; short-chain acyl-CoA hydrolase; short-chain acyl-CoA thioesterase
Systematic name: ADP-dependent-short-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117698-16-5
References:
1.  Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416]
2.  Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13–19. [DOI] [PMID: 2570608]
[EC 3.1.2.18 created 1992]
 
 
EC 3.1.2.19     
Accepted name: ADP-dependent medium-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): medium-chain acyl coenzyme A hydrolase; medium-chain acyl-CoA hydrolase; medium-chain acyl-thioester hydrolase; medium-chain hydrolase; myristoyl-CoA thioesterase
Systematic name: ADP-dependent-medium-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-75-7
References:
1.  Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416]
[EC 3.1.2.19 created 1992]
 
 
EC 3.1.2.20     
Accepted name: acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): acyl coenzyme A thioesterase; acyl-CoA thioesterase; acyl coenzyme A hydrolase; thioesterase B; thioesterase II; acyl-CoA thioesterase
Systematic name: acyl-CoA hydrolase
Comments: Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37270-64-7
References:
1.  Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13–19. [DOI] [PMID: 2570608]
[EC 3.1.2.20 created 1992]
 
 
EC 3.1.2.21     
Accepted name: dodecanoyl-[acyl-carrier-protein] hydrolase
Reaction: a dodecanoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + dodecanoate
Other name(s): lauryl-acyl-carrier-protein hydrolase; dodecanoyl-acyl-carrier-protein hydrolase; dodecyl-acyl-carrier protein hydrolase; dodecanoyl-[acyl-carrier protein] hydrolase; dodecanoyl-[acyl-carrier-protein] hydrolase
Systematic name: dodecanoyl-[acyl-carrier protein] hydrolase
Comments: Acts on the acyl-carrier-protein thioester of C12 and, with a much lower activity, C14 fatty acids. The derivative of oleic acid is hydrolysed very slowly (cf. EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 137903-37-8
References:
1.  Pollard, M.R., Anderson, L., Fan, C., Hawkins, D.J., Davies, H.M. A specific acyl-ACP thioesterase implicated in medium-chain fatty acid production in immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 284 (1991) 306–312. [DOI] [PMID: 1989513]
2.  Davies, H.M., Anderson, L., Fan, C., Hawkins, D.J. Developmental induction, purification, and further characterization of 12:0-ACP thioesterase from immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 290 (1991) 37–45. [DOI] [PMID: 1898097]
[EC 3.1.2.21 created 1999]
 
 
EC 3.1.2.22     
Accepted name: palmitoyl[protein] hydrolase
Reaction: palmitoyl[protein] + H2O = palmitate + protein
Other name(s): palmitoyl-protein thioesterase; palmitoyl-(protein) hydrolase
Systematic name: palmitoyl[protein] hydrolase
Comments: Specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 150605-49-5
References:
1.  Camp, L.A., Hofmann, S.L. Assay and isolation of palmitoyl-protein thioesterase from bovine brain using palmitoylated H-Ras as substrate. Methods Enzymol. 250 (1995) 336–347. [DOI] [PMID: 7651163]
2.  Schriner, J.E., Yi, W., Hofmann, S.L. cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics 34 (1996) 317–322. [DOI] [PMID: 8786130]
3.  Verkruyse, L.A., Hofmann, S.L. Lysosomal targeting of palmitoyl-protein thioesterase. J. Biol. Chem. 271 (1996) 15831–15836. [DOI] [PMID: 8663305]
[EC 3.1.2.22 created 1999]
 
 
EC 3.1.2.23     
Accepted name: 4-hydroxybenzoyl-CoA thioesterase
Reaction: 4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
Systematic name: 4-hydroxybenzoyl-CoA hydrolase
Comments: This enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 141583-19-9
References:
1.  Chang, K.H., Liang, P.H., Beck, W., Scholten, J.D., Dunaway-Mariano, D. Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3. Biochemistry 31 (1992) 5605–5610. [PMID: 1610806]
2.  Dunaway-Mariano, D., Babbitt, P.C. On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway. Biodegradation 5 (1994) 259–276. [PMID: 7765837]
[EC 3.1.2.23 created 1999]
 
 
EC 3.1.2.24      
Transferred entry: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase. Now EC 3.13.1.3, 2′-hydroxybiphenyl-2-sulfinate desulfinase. The enzyme was incorrectly classified as a thioester hydrolase when the bond broken is a C-S bond, which is not an ester
[EC 3.1.2.24 created 2000, deleted 2005]
 
 
EC 3.1.2.25     
Accepted name: phenylacetyl-CoA hydrolase
Reaction: phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA
For diagram of phenylacetyl-CoA metabolism, click here
Systematic name: phenylglyoxylyl-CoA hydrolase
Comments: This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 57219-72-4
References:
1.  Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507–515. [DOI] [PMID: 10336636]
2.  Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509–516. [PMID: 9575237]
[EC 3.1.2.25 created 2004]
 
 
EC 3.1.2.26      
Transferred entry: bile-acid-CoA hydrolase. Now EC 2.8.3.25, bile acid CoA transferase
[EC 3.1.2.26 created 2005, deleted 2016]
 
 
EC 3.1.2.27     
Accepted name: choloyl-CoA hydrolase
Reaction: choloyl-CoA + H2O = cholate + CoA
For diagram of the biosynthesis of cholic-acid conjugates, click here
Other name(s): PTE-2 (ambiguous); choloyl-coenzyme A thioesterase; chenodeoxycholoyl-coenzyme A thioesterase; peroxisomal acyl-CoA thioesterase 2
Systematic name: choloyl-CoA hydrolase
Comments: Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoAs, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoAs, all of which are present in peroxisomes. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hunt, M.C., Solaas, K., Kase, B.F. and Alexson, S.E. Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. J. Biol. Chem. 277 (2002) 1128–1138. [DOI] [PMID: 11673457]
2.  Solaas, K., Sletta, R.J., Soreide, O. and Kase, B.F. Presence of choloyl- and chenodeoxycholoyl-coenzyme A thioesterase activity in human liver. Scand. J. Clin. Lab. Invest. 60 (2000) 91–102. [PMID: 10817395]
3.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC 3.1.2.27 created 2005]
 
 
EC 3.1.2.28     
Accepted name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Reaction: 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA
For diagram of vitamin K biosynthesis, click here
Other name(s): menI (gene name); ydiL (gene name)
Systematic name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Comments: This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Muller, W. and Leistner, E. 1,4-Naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis. Phytochemistry 15 (1976) 407–410.
2.  Eichinger, D., Bacher, A., Zenk, M.H. and Eisenreich, W. Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum. J. Am. Chem. Soc. 121 (1999) 7469–7475.
3.  Widhalm, J.R., van Oostende, C., Furt, F. and Basset, G.J. A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. Proc. Natl. Acad. Sci. USA 106 (2009) 5599–5603. [DOI] [PMID: 19321747]
4.  Chen, M., Ma, X., Chen, X., Jiang, M., Song, H. and Guo, Z. Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. J. Bacteriol. 195 (2013) 2768–2775. [DOI] [PMID: 23564174]
[EC 3.1.2.28 created 2010]
 
 
EC 3.1.2.29     
Accepted name: fluoroacetyl-CoA thioesterase
Reaction: fluoroacetyl-CoA + H2O = fluoroacetate + CoA
Systematic name: fluoroacetyl-CoA hydrolase
Comments: Fluoroacetate is extremely toxic. It reacts with CoA to form fluoroacetyl-CoA, which substitutes for acetyl CoA and reacts with EC 2.3.3.1 (citrate synthase) to produce fluorocitrate, a metabolite of which binds very tightly to EC 4.2.1.3 (aconitase) and halts the TCA cycle. This enzyme hydrolyses fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance on the organisms that produce it. It has been described in the poisonous plant Dichapetalum cymosum and the bacterium Streptomyces cattleya, both of which are fluoroacetate producers.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meyer, J.J.M., Grobbelaar, N., Vleggaar, R. and Louw, A.I. Fluoroacetyl-coenzyme-A hydrolase-like activity in Dichapetalum cymosum. J. Plant Physiol. 139 (1992) 369–372.
2.  Huang, F., Haydock, S.F., Spiteller, D., Mironenko, T., Li, T.L., O'Hagan, D., Leadlay, P.F. and Spencer, J.B. The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A. Chem. Biol. 13 (2006) 475–484. [DOI] [PMID: 16720268]
3.  Dias, M.V., Huang, F., Chirgadze, D.Y., Tosin, M., Spiteller, D., Dry, E.F., Leadlay, P.F., Spencer, J.B. and Blundell, T.L. Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK. J. Biol. Chem. 285 (2010) 22495–22504. [DOI] [PMID: 20430898]
[EC 3.1.2.29 created 2011]
 
 
EC 3.1.2.30     
Accepted name: (3S)-malyl-CoA thioesterase
Reaction: (S)-malyl-CoA + H2O = (S)-malate + CoA
Glossary: (S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): mcl2 (gene name)
Systematic name: (S)-malyl-CoA hydrolase
Comments: Stimulated by Mg2+ or Mn2+. The enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erb, T.J., Frerichs-Revermann, L., Fuchs, G. and Alber, B.E. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192 (2010) 1249–1258. [DOI] [PMID: 20047909]
[EC 3.1.2.30 created 2014]
 
 
EC 3.1.2.31     
Accepted name: dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase
Reaction: dihydromonacolin L-[lovastatin nonaketide synthase] + H2O = holo-[lovastatin nonaketide synthase] + dihydromonacolin L acid
For diagram of lovastatin biosynthesis, click here
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovG
Systematic name: dihydromonacolin L-[lovastatin nonaketide synthase] hydrolase
Comments: Dihydromonacolin L acid is synthesized while bound to an acyl-carrier protein domain of the lovastatin nonaketide synthase (EC 2.3.1.161). Since that enzyme lacks a thioesterase domain, release of the dihydromonacolin L acid moiety from the polyketide synthase requires this dedicated enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xu, W., Chooi, Y.H., Choi, J.W., Li, S., Vederas, J.C., Da Silva, N.A. and Tang, Y. LovG: the thioesterase required for dihydromonacolin L release and lovastatin nonaketide synthase turnover in lovastatin biosynthesis. Angew. Chem. Int. Ed. Engl. 52 (2013) 6472–6475. [DOI] [PMID: 23653178]
[EC 3.1.2.31 created 2015]
 
 
EC 3.1.2.32     
Accepted name: 2-aminobenzoylacetyl-CoA thioesterase
Reaction: (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA
Other name(s): pqsE (gene name)
Systematic name: (2-aminobenzoyl)acetyl-CoA hydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yu, S., Jensen, V., Seeliger, J., Feldmann, I., Weber, S., Schleicher, E., Haussler, S. and Blankenfeldt, W. Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry 48 (2009) 10298–10307. [DOI] [PMID: 19788310]
2.  Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611–618. [DOI] [PMID: 25960261]
[EC 3.1.2.32 created 2016]
 
 


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