The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version

EC 3.1.1.11     
Accepted name: pectinesterase
Reaction: pectin + n H2O = n methanol + pectate
Other name(s): pectin demethoxylase; pectin methoxylase; pectin methylesterase; pectase; pectin methyl esterase; pectinoesterase
Systematic name: pectin pectylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-98-3
References:
1.  Deuel, H. and Stutz, E. Pectic substances and pectic enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341–382. [PMID: 13605988]
2.  Lineweaver, H. and Jansen, E.F. Pectic enzymes. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 267–295.
3.  Mills, G.B. A biochemical study of Pseudomonas prunicola Wormald. I. Pectin esterase. Biochem. J. 44 (1949) 302–305. [PMID: 16748520]
[EC 3.1.1.11 created 1961]
 
 
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]
 
 


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