The Enzyme Database

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
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:
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, PDB
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, PDB
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, PDB
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
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
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. [DOI] [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, PDB
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
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
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:
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, PDB
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, PDB
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, PDB
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 3.1.1.119      
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 3.1.1.119 created 2022, deleted 2022]
 
 
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:
1.  Hobbs, M.E., Vetting, M., Williams, H.J., Narindoshvili, T., Kebodeaux, D.M., Hillerich, B., Seidel, R.D., Almo, S.C. and Raushel, F.M. Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry 52 (2013) 239–253. [DOI] [PMID: 23214453]
[EC 3.1.1.120 created 2022]
 
 
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:
1.  Yakobov, N., Fischer, F., Mahmoudi, N., Saga, Y., Grube, C.D., Roy, H., Senger, B., Grob, G., Tatematsu, S., Yokokawa, D., Mouyna, I., Latge, J.P., Nakajima, H., Kushiro, T. and Becker, H.D. RNA-dependent sterol aspartylation in fungi. Proc. Natl. Acad. Sci. USA 117 (2020) 14948–14957. [DOI] [PMID: 32541034]
[EC 3.1.1.121 created 2023]
 
 
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)
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:
1.  Pandey, G., Dorrian, S.J., Russell, R.J., Brearley, C., Kotsonis, S. and Oakeshott, J.G. Cloning and biochemical characterization of a novel carbendazim (methyl-1H-benzimidazol-2-ylcarbamate)-hydrolyzing esterase from the newly isolated Nocardioides sp. strain SG-4G and its potential for use in enzymatic bioremediation. Appl. Environ. Microbiol. 76 (2010) 2940–2945. [DOI] [PMID: 20228105]
[EC 3.1.1.122 created 2023]
 
 


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