The Enzyme Database

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EC 3.1.1.7     
Accepted name: acetylcholinesterase
Reaction: acetylcholine + H2O = choline + acetate
Other name(s): true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl.β-methylcholinesterase; AcCholE
Systematic name: acetylcholine acetylhydrolase
Comments: Acts on a variety of acetic esters; also catalyses transacetylations.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9000-81-1
References:
1.  Augustinsson, K.-B. Cholinesterases. A study in comparative enzymology. Acta Physiol. Scand. 15, Suppl. 2 (1948) .
2.  Bergmann, F., Rimon, S. and Segal, R. Effect of pH on the activity of eel esterase towards different substrates. Biochem. J. 68 (1958) 493–499. [PMID: 13522650]
3.  Cilliv, G. and Ozand, P.T. Human erythrocyte acetylcholinesterase purification, properties and kinetic behavior. Biochim. Biophys. Acta 284 (1972) 136–156. [DOI] [PMID: 5073758]
4.  Leuzinger, W., Baker, A.L. and Cauvin, E. Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point. Proc. Natl. Acad. Sci. USA 59 (1968) 620–623. [DOI] [PMID: 5238989]
5.  Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259–339. [PMID: 14885021]
6.  Zittle, C.A., DellaMonica, E.S., Custer, J.H. and Krikorian, R. Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction. Arch. Biochem. Biophys. 56 (1955) 469–475. [DOI] [PMID: 14377597]
[EC 3.1.1.7 created 1961]
 
 
EC 3.1.1.70     
Accepted name: cetraxate benzylesterase
Reaction: cetraxate benzyl ester + H2O = cetraxate + benzyl alcohol
Systematic name: cetraxate-benzyl-ester benzylhydrolase
Comments: Acts on a number of benzyl esters of substituted phenyl propanoates, and on the benzyl esters of phenylalanine and tyrosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125858-78-8
References:
1.  Kuroda, H., Miyadera, A., Imura, A. and Suzuki, A. Partial purification, and some properties and reactivities of cetraxate benzyl ester hydrochloride-hydrolyzing enzyme. Chem. Pharm. Bull. 37 (1989) 2929–2932. [PMID: 2632040]
[EC 3.1.1.70 created 1992]
 
 
EC 3.1.1.71     
Accepted name: acetylalkylglycerol acetylhydrolase
Reaction: 2-acetyl-1-alkyl-sn-glycerol + H2O = 1-alkyl-sn-glycerol + acetate
Other name(s): alkylacetylglycerol acetylhydrolase
Systematic name: 2-acetyl-1-alkyl-sn-glycerol acetylhydrolase
Comments: Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. The enzyme from Erlich ascites cells is membrane-bound. It differs from lipoprotein lipase (EC 3.1.1.34) since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Blank, M.L., Smith, Z.L., Cress, E.A., Snyder, F. Characterization of the enzymatic hydrolysis of acetate from alkylacetylglycerols in the de novo pathway of PAF biosynthesis. Biochim. Biophys. Acta 1042 (1990) 153–158. [DOI] [PMID: 2302414]
[EC 3.1.1.71 created 1999]
 
 
EC 3.1.1.72     
Accepted name: acetylxylan esterase
Reaction: Deacetylation of xylans and xylo-oligosaccharides
Systematic name: acetylxylan esterase
Comments: Catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, α-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 188959-24-2
References:
1.  Sundberg, M., Poutanen, K. Purification and properties of two acetylxylan esterases of Trichoderma reesei. Biotechnol. Appl. Biochem. 13 (1991) 1–11.
2.  Poutanen, K., Sundberg, M., Korte, H., Puls, J. Deacetylation of xylans by acetyl esterases of Trichoderma reesei. Appl. Microbiol. Biotechnol. 33 (1990) 506–510.
3.  Margolles-Clark, E., Tenkanen, M., Söderland, H., Penttilä, M. Acetyl xylan esterase from Trichoderma reesei contains an active site serine and a cellulose binding domain. Eur. J. Biochem. 237 (1996) 553–560. [DOI] [PMID: 8647098]
[EC 3.1.1.72 created 1999]
 
 
EC 3.1.1.73     
Accepted name: feruloyl esterase
Reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide
Glossary: ferulate = 4-hydroxy-3-methoxycinnamate
Other name(s): ferulic acid esterase, hydroxycinnamoyl esterase, hemicellulase accessory enzymes; FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, FAE-II
Systematic name: 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase
Comments: Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates. p-Nitrophenol acetate and methyl ferulate are poorer substrates. All microbial ferulate esterases are secreted into the culture medium. They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 134712-49-5
References:
1.  Faulds, C.B. and Williamson, G. The purification and characterisation of 4-hydroxy-3-methoxy-cinnamic (ferulic) acid esterase from Streptomyces olivochromogenes (3232). J. Gen. Microbiol. 137 (1991) 2339–2345. [DOI] [PMID: 1663152]
2.  Faulds, C.B. and Williamson, G. Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger. Specificity for the phenolic moiety and binding to microcrystalline cellulose. Microbiology 140 (1994) 779–787.
3.  Kroon, P.A., Faulds, C.B. and Williamson, G. Purification and characterisation of a novel ferulic acid esterase induced by growth of Aspergillus niger on sugarbeet pulp. Biotechnol. Appl. Biochem. 23 (1996) 255–262. [PMID: 8679110]
4.  deVries, R.P. , Michelsen,B., Poulsen, C.H., Kroon, P.A., van den Heuvel, R.H.H., Faulds, C.B., Williamson, G., van den Homberg, J.P.T.W. and Visser, J. The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides. Appl. Environ. Microbiol. 63 (1997) 4638–4644. [PMID: 9406381]
5.  Castanares, A., Mccrae, S.I. and Wood, T.M. Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme Microbiol. Technol. 14 (1992) 875–884.
[EC 3.1.1.73 created 2000]
 
 
EC 3.1.1.74     
Accepted name: cutinase
Reaction: cutin + H2O = cutin monomers
Systematic name: cutin hydrolase
Comments: Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51377-41-4
References:
1.  Garcia-Lepe, R., Nuero, O.M., Reyes, F. and Santamaria, F. Lipases in autolysed cultures of filamentous fungi. Lett. Appl. Microbiol. 25 (1997) 127–130. [DOI] [PMID: 9281862]
2.  Purdy, R.E. and Kolattukudy, P.E. Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 14 (1975) 2824–2831. [PMID: 1156575]
3.  Purdy, R.E. and Kolattukudy, P.E. Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry 14 (1975) 2832–2840. [PMID: 239740]
[EC 3.1.1.74 created 2000]
 
 
EC 3.1.1.75     
Accepted name: poly(3-hydroxybutyrate) depolymerase
Reaction: [(R)-3-hydroxybutanoate]n + H2O = [(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x; x = 1–5
Other name(s): PHB depolymerase; poly(3HB) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HASCL) depolymerase; poly[(R)-3-hydroxybutyrate] hydrolase
Systematic name: poly[(R)-3-hydroxybutanoate] hydrolase
Comments: Reaction also occurs with esters of other short-chain-length (C1-C5) hydroxyalkanoic acids (HA). There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-11-3
References:
1.  Jendrossek, D. Microbial degradation of polyesters. Adv. Biochem. Eng./Biotechnol. 71 (2001) 293–325. [PMID: 11217416]
2.  García, B., Olivera, E.R., Miñambres, B., Fernández-Valverde, Cañedo, L.M., Prieto, M.A., García, J.L., Martínez, M. and Luengo, J.M. Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-CoA catabolon. J. Biol. Chem. 274 (1999) 29228–29241. [DOI] [PMID: 10506180]
[EC 3.1.1.75 created 2001]
 
 
EC 3.1.1.76     
Accepted name: poly(3-hydroxyoctanoate) depolymerase
Reaction: Hydrolyses the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to oligomers
Other name(s): PHO depolymerase; poly(3HO) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HAMCL) depolymerase; poly[(R)-3-hydroxyoctanoate] hydrolase
Systematic name: poly{oxycarbonyl[(R)-2-pentylethylene]} hydrolase
Comments: The main product after prolonged incubation is the dimer [3]. Besides hydrolysing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyses other polymers derived from medium-chain-length (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these. It also hydrolyses p-nitrophenyl esters of fatty acids. Polymers of short-chain-length hydroxyalkanoic acids such as poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic acid] are not hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jendrossek, D. Microbial degradation of polyesters. Adv. Biochem. Eng./Biotechnol. 71 (2001) 293–325. [PMID: 11217416]
2.  García, B., Olivera, E.R., Miñambres, B., Fernández-Valverde, Cañedo, L.M., Prieto, M.A., García, J.L., Martínez, M. and Luengo, J.M. Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-CoA catabolon. J. Biol. Chem. 274 (1999) 29228–29241. [DOI] [PMID: 10506180]
3.  Schirmer, A., Jendrossek, D. and Schlegel, H.G. Degradation of poly(3-hydroxyoctanoic acid) [P(3HO)] by bacteria: purification and properties of a P(3HO) depolymerase from Pseudomonas fluorescens GK13. Appl. Environ. Microbiol. 59 (1993) 1220–1227. [PMID: 8476295]
[EC 3.1.1.76 created 2001, modified 2005]
 
 
EC 3.1.1.77     
Accepted name: acyloxyacyl hydrolase
Reaction: 3-(acyloxy)acyl group of bacterial toxin + H2O = 3-hydroxyacyl group of bacterial toxin + a fatty acid
For diagram of reaction, click here
Comments: The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, β-D-GlcN-(1→ 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 110277-64-0
References:
1.  Erwin, A.L. and Munford, R.S. Deacylation of structurally diverse lipopolysaccharides by human acyloxyacyl hydrolase. J. Biol. Chem. 265 (1990) 16444–16449. [PMID: 2398058]
2.  Hagen, F.S., Grant, F.J., Kuijper, J.L., Slaughter, C.A., Moomaw, C.R., Orth, K., O'Hara, P.J. and Munford, R.S. Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides. Biochemistry 30 (1991) 8415–8423. [PMID: 1883828]
3.  Munford, R.S. and Hunter, J.P. Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro. J. Biol. Chem. 267 (1992) 10116–10121. [PMID: 1577781]
[EC 3.1.1.77 created 2001]
 
 
EC 3.1.1.78     
Accepted name: polyneuridine-aldehyde esterase
Reaction: polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol
For diagram of geissoschizine and sarpagine biosynthesis, click here
Other name(s): polyneuridine aldehyde esterase; PNAE
Systematic name: polyneuridine aldehyde hydrolase (decarboxylating)
Comments: Following hydrolysis of this indole alkaloid ester the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton. The enzyme also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87041-55-2
References:
1.  Pfitzner, A. and Stöckigt, J. Characterization of polyneuridine aldehyde esterase, a key enzyme in the biosynthesis of sarpagine ajmaline type alkaloids. Planta Med. 48 (1983) 221–227. [PMID: 17404987]
2.  Pfitzner, A. and Stöckigt, J. Polyneuridine aldehyde esterase: an unusual specific enzyme involved in the biosynthesis of sarpagine type alkaloids. J. Chem. Soc. Chem. Commun. (1983) 459–460.
3.  Dogru, E., Warzecha, H., Seibel, F., Haebel, S., Lottspeich, F. and Stöckigt, J. The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of the hydrolase super family. Eur. J. Biochem. 267 (2000) 1397–1406. [DOI] [PMID: 10691977]
4.  Mattern-Dogru, E., Ma, X., Hartmann, J., Decker, H. and Stöckigt, J. Potential active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesis. Eur. J. Biochem. 269 (2002) 2889–2896. [DOI] [PMID: 12071952]
[EC 3.1.1.78 created 2002]
 
 
EC 3.1.1.79     
Accepted name: hormone-sensitive lipase
Reaction: (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
(2) triacylglycerol + H2O = diacylglycerol + a carboxylate
(3) monoacylglycerol + H2O = glycerol + a carboxylate
Other name(s): HSL
Systematic name: diacylglycerol acylhydrolase
Comments: This enzyme is a serine hydrolase. Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity. It hydrolyses all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) [2,3,4] as well as cholesteryl esters [2,4], steroid fatty acid esters [5], retinyl esters [6] and p-nitrophenyl esters [4,7]. It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond [8]. The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length. The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Holm, C., Osterlund, T., Laurell, H. and Contreras, J.A. Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Annu. Rev. Nutr. 20 (2000) 365–393. [DOI] [PMID: 10940339]
2.  Fredrikson, G., Stralfors, P., Nilsson, N.O. and Belfrage, P. Hormone-sensitive lipase of rat adipose tissue. Purification and some properties. J. Biol. Chem. 256 (1981) 6311–6320. [PMID: 7240206]
3.  Vaughan, M., Berger, J.E. and Steinberg, D. Hormone-sensitive lipase and monoglyceride lipase activities in adipose tissue. J. Biol. Chem. 239 (1964) 401–409. [PMID: 14169138]
4.  Østerlund, T., Danielsson, B., Degerman, E., Contreras, J.A., Edgren, G., Davis, R.C., Schotz, M.C. and Holm, C. Domain-structure analysis of recombinant rat hormone-sensitive lipase. Biochem. J. 319 ( Pt 2) (1996) 411–420. [PMID: 8912675]
5.  Lee, F.T., Adams, J.B., Garton, A.J. and Yeaman, S.J. Hormone-sensitive lipase is involved in the hydrolysis of lipoidal derivatives of estrogens and other steroid hormones. Biochim. Biophys. Acta 963 (1988) 258–264. [DOI] [PMID: 3196730]
6.  Wei, S., Lai, K., Patel, S., Piantedosi, R., Shen, H., Colantuoni, V., Kraemer, F.B. and Blaner, W.S. Retinyl ester hydrolysis and retinol efflux from BFC-1β adipocytes. J. Biol. Chem. 272 (1977) 14159–14165. [DOI] [PMID: 9162045]
7.  Tsujita, T., Ninomiya, H. and Okuda, H. p-Nitrophenyl butyrate hydrolyzing activity of hormone-sensitive lipase from bovine adipose tissue. J. Lipid Res. 30 (1989) 997–1004. [PMID: 2794798]
8.  Yeaman, S.J. Hormone-sensitive lipase - new roles for an old enzyme. Biochem. J. 379 (2004) 11–22. [DOI] [PMID: 14725507]
[EC 3.1.1.79 created 2004]
 
 


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