The Enzyme Database

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EC 3.1.1.1     
Accepted name: carboxylesterase
Reaction: a carboxylic ester + H2O = an alcohol + a carboxylate
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase
Systematic name: carboxylic-ester hydrolase
Comments: Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9016-18-6
References:
1.  Augusteyn, R.C., de Jersey, J., Webb, E.C. and Zerner, B. On the homology of the active-site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171 (1969) 128–137. [DOI] [PMID: 4884138]
2.  Barker, D.L. and Jencks, W.P. Pig liver esterase. Physical properties. Biochemistry 8 (1969) 3879–3889. [PMID: 4981346]
3.  Bertram, J. and Krisch, K. Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney. Eur. J. Biochem. 11 (1969) 122–126. [DOI] [PMID: 5353595]
4.  Burch, J. The purification and properties of horse liver esterase. Biochem. J. 58 (1954) 415–426. [PMID: 13208632]
5.  Horgan, D.J., Stoops, J.K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase. Biochemistry 8 (1969) 2000–2006. [PMID: 5785220]
6.  Malhotra, O.P. and Philip, G. Specificity of goat intestinal esterase. Biochem. Z. 346 (1966) 386–402.
7.  Mentlein, R., Schumann, M. and Heymann, E. Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes. Arch. Biochem. Biophys. 234 (1984) 612–621. [DOI] [PMID: 6208846]
8.  Runnegar, M.T.C., Scott, K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase. Biochemistry 8 (1969) 2013–2018. [PMID: 5785222]
[EC 3.1.1.1 created 1961]
 
 
EC 3.1.1.2     
Accepted name: arylesterase
Reaction: a phenyl acetate + H2O = a phenol + acetate
Other name(s): A-esterase (ambiguous); paraoxonase (ambiguous); aromatic esterase
Systematic name: aryl-ester hydrolase
Comments: Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (±)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [8].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9032-73-9
References:
1.  Aldridge, W.N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53 (1953) 110–117. [PMID: 13032041]
2.  Augustinsson, K.-B. and Olsson, B. Esterases in the milk and blood plasma of swine. 1. Substrate specificity and electrophoresis studies. Biochem. J. 71 (1959) 477–484. [PMID: 13638253]
3.  Bosmann, H.B. Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate. Biochim. Biophys. Acta 276 (1972) 180–191. [DOI] [PMID: 5047702]
4.  Kim, D.-H., Yang, Y.-S. and Jakoby, W.B. Nonserine esterases from rat liver cytosol. Protein Expr. Purif. 1 (1990) 19–27. [DOI] [PMID: 2152179]
5.  Mackness, M.I., Thompson, H.M., Hardy, A.R. and Walker, C.H. Distinction between 'A′-esterases and arylesterases. Implications for esterase classification. Biochem. J. 245 (1987) 293–296. [PMID: 2822017]
6.  Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Ed.), Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989.
7.  Khersonsky, O. and Tawfik, D.S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44 (2005) 6371–6382. [DOI] [PMID: 15835926]
8.  Draganov, D.I., Teiber, J.F., Speelman, A., Osawa, Y., Sunahara, R. and La Du, B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46 (2005) 1239–1247. [DOI] [PMID: 15772423]
[EC 3.1.1.2 created 1961, modified 1989]
 
 
EC 3.1.1.3     
Accepted name: triacylglycerol lipase
Reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): lipase (ambiguous); butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; PNLIP (gene name); LIPF (gene name)
Systematic name: triacylglycerol acylhydrolase
Comments: The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
Links to other databases: BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-62-1
References:
1.  Singer, T.P. and Hofstee, B.H.J. Studies on wheat germ lipase. I. Methods of estimation, purification and general properties of the enzyme. Arch. Biochem. 18 (1948) 229–243. [PMID: 18875045]
2.  Singer, T.P. and Hofstee, B.H.J. Studies on wheat germ lipase. II. Kinetics. Arch. Biochem. 18 (1948) 245–259. [PMID: 18875046]
3.  Sarda, L. and Desnuelle, P. Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta 30 (1958) 513–521. [DOI] [PMID: 13618257]
4.  Lynn, W.S. and Perryman, N.C. Properties and purification of adipose tissue lipase. J. Biol. Chem. 235 (1960) 1912–1916. [PMID: 14419169]
5.  Paznokas, J.L. and Kaplan, A. Purification and properties of a triacylglycerol lipase from Mycobacterium phlei. Biochim. Biophys. Acta 487 (1977) 405–421. [PMID: 18200]
6.  Tiruppathi, C. and Balasubramanian, K.A. Purification and properties of an acid lipase from human gastric juice. Biochim. Biophys. Acta 712 (1982) 692–697. [PMID: 7126632]
7.  Hills, M.J. and Mukherjee, K.D. Triacylglycerol lipase from rape (Brassica napus L.) suitable for biotechnological purposes. Appl. Biochem. Biotechnol. 26 (1990) 1–10. [PMID: 2268143]
8.  Winkler, F.K., D'Arcy, A. and Hunziker, W. Structure of human pancreatic lipase. Nature 343 (1990) 771–774. [PMID: 2106079]
9.  Kim, K.K., Song, H.K., Shin, D.H., Hwang, K.Y. and Suh, S.W. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure 5 (1997) 173–185. [PMID: 9032073]
10.  Kurat, C.F., Natter, K., Petschnigg, J., Wolinski, H., Scheuringer, K., Scholz, H., Zimmermann, R., Leber, R., Zechner, R. and Kohlwein, S.D. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J. Biol. Chem. 281 (2006) 491–500. [PMID: 16267052]
11.  Ranaldi, S., Belle, V., Woudstra, M., Bourgeas, R., Guigliarelli, B., Roche, P., Vezin, H., Carriere, F. and Fournel, A. Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics. Biochemistry 49 (2010) 2140–2149. [PMID: 20136147]
[EC 3.1.1.3 created 1961]
 
 
EC 3.1.1.4     
Accepted name: phospholipase A2
Reaction: phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Other name(s): lecithinase A; phosphatidase; phosphatidolipase; phospholipase A
Systematic name: phosphatidylcholine 2-acylhydrolase
Comments: Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-84-7
References:
1.  Doery, H.M. and Pearson, J.E. Haemolysins in venoms of Australian snakes. Observations on the haemolysins of the venoms of some Australian snakes and the separation of phospholipase A from the venom of Pseudechis porphyriacus. Biochem. J. 78 (1961) 820–827. [PMID: 13723433]
2.  Fraenkel-Conrat, H. and Fraenkel-Conrat, J. Inactivation of crotoxin by group-specific reagents. Biochim. Biophys. Acta 5 (1950) 98–104. [DOI] [PMID: 15433984]
3.  Hanahan, D.J., Brockerhoff, H. and Barron, E.J. The site of attack of phospholipase (lecithinase) A on lecithin: a re-evaluation. Position of fatty acids on lecithins and triglycerides. J. Biol. Chem. 235 (1960) 1917–1923. [PMID: 14399412]
4.  Moore, J.H. and Williams, D.L. Some observations on the specificity of phospholipase A. Biochim. Biophys. Acta 84 (1964) 41–54. [PMID: 14124755]
5.  Saito, K. and Hanahan, D.J. A study of the purification and properties of the phospholipase A of Crotalus adamanteus venom. Biochemistry 1 (1962) 521–532. [PMID: 14496116]
6.  van den Bosch, H. Intracellular phospholipases A. Biochim. Biophys. Acta 604 (1980) 191–246. [DOI] [PMID: 6252969]
[EC 3.1.1.4 created 1961, modified 1976, modified 1983]
 
 
EC 3.1.1.5     
Accepted name: lysophospholipase
Reaction: 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Other name(s): lecithinase B; lysolecithinase; phospholipase B; lysophosphatidase; lecitholipase; phosphatidase B; lysophosphatidylcholine hydrolase; lysophospholipase A1; lysophopholipase L2; lysophospholipase transacylase; neuropathy target esterase; NTE; NTE-LysoPLA; NTE-lysophospholipase
Systematic name: 2-lysophosphatidylcholine acylhydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-85-8
References:
1.  Abe, M., Ohno, K. and Sato, R. Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction. Biochim. Biophys. Acta 369 (1974) 361–370.
2.  Contardi, A. and Ercoli, A. The enzymic cleavage of lecithin and lysolecithin. Biochem. Z. 261 (1933) 275–302.
3.  Dawson, R.M.C. Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation. Biochem. J. 70 (1958) 559–570. [PMID: 13607409]
4.  Fairbairn, D. The preparation and properties of a lysophospholipase from Penicillium notatum. J. Biol. Chem. 173 (1948) 705–714. [PMID: 18910725]
5.  Shapiro, B. Purification and properties of a lysolecithinase from pancreas. Biochem. J. 53 (1953) 663–666. [PMID: 13032127]
6.  van den Bosch, H., Aarsman, A.J., De Jong, J.G.N. and van Deenen, L.L.M. Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas. Biochim. Biophys. Acta 296 (1973) 94–104. [DOI] [PMID: 4693514]
7.  van den Bosch, H., Vianen, G.M. and van Heusden, G.P.H. Lysophospholipase-transacylase from rat lung. Methods Enzymol. 71 (1981) 513–521. [PMID: 7278668]
8.  van Tienhoven, M., Atkins, J., Li, Y. and Glynn, P. Human neuropathy target esterase catalyzes hydrolysis of membrane lipids. J. Biol. Chem. 277 (2002) 20942–20948. [DOI] [PMID: 11927584]
9.  Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E. and Casida, J.E. Evidence that mouse brain neuropathy target esterase is a lysophospholipase. Proc. Natl. Acad. Sci. USA 100 (2003) 7983–7987. [DOI] [PMID: 12805562]
10.  Lush, M.J., Li, Y., Read, D.J., Willis, A.C. and Glynn, P. Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man. Biochem. J. 332 (1998) 1–4. [PMID: 9576844]
11.  Winrow, C.J., Hemming, M.L., Allen, D.M., Quistad, G.B., Casida, J.E. and Barlow, C. Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity. Nat. Genet. 33 (2003) 477–485. [DOI] [PMID: 12640454]
[EC 3.1.1.5 created 1961, modified 1976, modified 1983]
 
 
EC 3.1.1.6     
Accepted name: acetylesterase
Reaction: an acetic ester + H2O = an alcohol + acetate
For diagram of peraksine biosynthesis, click here
Other name(s): C-esterase (in animal tissues); acetic ester hydrolase; chloroesterase; p-nitrophenyl acetate esterase; Citrus acetylesterase
Systematic name: acetic-ester acetylhydrolase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9000-82-2
References:
1.  Aldridge, W.N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53 (1953) 110–117. [PMID: 13032041]
2.  Bergmann, F. and Rimon, S. Fractionation of C-esterase from the hog's kidney extract. Biochem. J. 77 (1960) 209–214. [PMID: 16748846]
3.  Jansen, E.F., Nutting, M.-D.F. and Balls, A.K. The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate. J. Biol. Chem. 175 (1948) 975–987. [PMID: 18880795]
[EC 3.1.1.6 created 1961]
 
 
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, Gene, 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 3.1.1.8     
Accepted name: cholinesterase
Reaction: an acylcholine + H2O = choline + a carboxylate
Other name(s): pseudocholinesterase; butyrylcholine esterase; non-specific cholinesterase; choline esterase II (unspecific); benzoylcholinesterase; choline esterase; butyrylcholinesterase; propionylcholinesterase; BtChoEase
Systematic name: acylcholine acylhydrolase
Comments: Acts on a variety of choline esters and a few other compounds.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-08-5
References:
1.  Augustinsson, K.-B. Cholinesterases. A study in comparative enzymology. Acta Physiol. Scand. 15, Suppl. 2 (1948) .
2.  Augustinsson, K.-B. and Olsson, B. Esterases in the milk and blood plasma of swine. 1. Substrate specificity and electrophoresis studies. Biochem. J. 71 (1959) 477–484. [PMID: 13638253]
3.  Koelle, G.B. Cholinesterases of the tissues and sera of rabbits. Biochem. J. 53 (1953) 217–226. [PMID: 13032058]
4.  Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259–339. [PMID: 14885021]
5.  Sawyer, C.H. Hydrolysis of choline esters by liver. Science 101 (1945) 385–386. [PMID: 17780326]
6.  Strelitz, F. Studies on cholinesterase. 4. Purification of pseudo-cholinesterase from horse serum. Biochem. J. 38 (1944) 86–88. [PMID: 16747753]
[EC 3.1.1.8 created 1961]
 
 
EC 3.1.1.9      
Deleted entry:  benzoylcholinesterase; a side reaction of EC 3.1.1.8 cholinesterase
[EC 3.1.1.9 created 1961, deleted 1972]
 
 
EC 3.1.1.10     
Accepted name: tropinesterase
Reaction: atropine + H2O = tropine + tropate
Other name(s): tropine esterase; atropinase; atropine esterase
Systematic name: atropine acylhydrolase
Comments: Also acts on cocaine and other tropine esters.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 59536-71-9
References:
1.  Glick, D., Glaubach, S. and Moore, D.H. Azolesterase activities of electrophoretically separated proteins of serum. J. Biol. Chem. 144 (1942) 525–528.
2.  Moog, P. and Krisch, K. [The purification and characterization of atropine esterase from rabbit liver microsomes] Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 529–542. [PMID: 4435736]
[EC 3.1.1.10 created 1961, deleted 1972, reinstated 1976]
 
 
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, Gene, 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 3.1.1.12      
Deleted entry:  vitamin A esterase, now believed to be identical with EC 3.1.1.1 carboxylesterase
[EC 3.1.1.12 created 1961, deleted 1972]
 
 
EC 3.1.1.13     
Accepted name: sterol esterase
Reaction: a steryl ester + H2O = a sterol + a fatty acid
Other name(s): cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase
Systematic name: steryl-ester acylhydrolase
Comments: A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-00-0
References:
1.  Hyun, J., Kothari, H., Herm, E., Mortenson, J., Treadwell, C.R. and Vahouny, G.V. Purification and properties of pancreatic juice cholesterol esterase. J. Biol. Chem. 244 (1969) 1937–1945. [PMID: 5780846]
2.  Okawa, Y. and Yamaguchi, T. Studies on sterol-ester hydrolase from Fusarium oxysporum. I. Partial purification and properties. J. Biochem. (Tokyo) 81 (1977) 1209–1215. [PMID: 19426]
3.  Vahouny, G.V. and Tradwell, C.R. Enzymatic synthesis and hydrolysis of cholesterol esters. Methods Biochem. Anal. 16 (1968) 219–272. [PMID: 4877146]
4.  Warnaar, F. Triterpene ester synthesis in latex of Euphorbia species. Phytochemistry 26 (1987) 2715–2721.
[EC 3.1.1.13 created 1961, modified 1990]
 
 
EC 3.1.1.14     
Accepted name: chlorophyllase
Reaction: chlorophyll + H2O = phytol + chlorophyllide
For diagram of chlorophyll catabolism, click here
Other name(s): CLH; Chlase
Systematic name: chlorophyll chlorophyllidohydrolase
Comments: Chlorophyllase has been found in higher plants, diatoms, and in the green algae Chlorella [3]. This enzyme forms part of the chlorophyll degradation pathway and is thought to take part in de-greening processes such as fruit ripening, leaf senescence and flowering, as well as in the turnover and homeostasis of chlorophyll [4]. This enzyme acts preferentially on chlorophyll a but will also accept chlorophyll b and pheophytins as substrates [5]. Ethylene and methyl jasmonate, which are known to accelerate senescence in many species, can enhance the activity of the hormone-inducible form of this enzyme [5].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-96-1
References:
1.  Holden, M. The breakdown of chlorophyll by chlorophyllase. Biochem. J. 78 (1961) 359–364. [PMID: 13715233]
2.  Klein, A.O. and Vishniac, W. Activity and partial purification of chlorophyllase in aqueous systems. J. Biol. Chem. 236 (1961) 2544–2547. [PMID: 13756631]
3.  Tsuchiya, T., Ohta, H., Okawa, K., Iwamatsu, A., Shimada, H., Masuda, T. and Takamiya, K. Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: finding of a lipase motif and the induction by methyl jasmonate. Proc. Natl. Acad. Sci. USA 96 (1999) 15362–15367. [DOI] [PMID: 10611389]
4.  Okazawa, A., Tango, L., Itoh, Y., Fukusaki, E. and Kobayashi, A. Characterization and subcellular localization of chlorophyllase from Ginkgo biloba. Z. Naturforsch. [C] 61 (2006) 111–117. [PMID: 16610227]
5.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
[EC 3.1.1.14 created 1961, modified 2007]
 
 
EC 3.1.1.15     
Accepted name: L-arabinonolactonase
Reaction: L-arabinono-1,4-lactone + H2O = L-arabinonate
For diagram of arabinose catabolism, click here
Systematic name: L-arabinono-1,4-lactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9025-95-0
References:
1.  Weimberg, R. and Doudoroff, M. The oxidation of L-arabinose by Pseudomonas saccharophila. J. Biol. Chem. 217 (1955) 607–624. [PMID: 13271422]
[EC 3.1.1.15 created 1961]
 
 
EC 3.1.1.16      
Deleted entry:  4-carboxymethyl-4-hydroxyisocrotonolactonase. This reaction was due to a mixture of EC 5.3.3.4 (muconolactone Δ-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase)
[EC 3.1.1.16 created 1961, deleted 1972]
 
 
EC 3.1.1.17     
Accepted name: gluconolactonase
Reaction: D-glucono-1,5-lactone + H2O = D-gluconate
For diagram of the mammalian ascorbic-acid biosynthesis pathway, click here
Other name(s): lactonase; aldonolactonase; glucono-δ-lactonase; gulonolactonase
Systematic name: D-glucono-1,5-lactone lactonohydrolase
Comments: Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed separately.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9012-73-1
References:
1.  Brodie, A.F. and Lipmann, F. Identification of a gluconolactonase. J. Biol. Chem. 212 (1955) 677–685. [PMID: 14353869]
2.  Bublitz, C. and Lehninger, A.L. The role of aldonolactonase in the conversion of L-gulonate to L-ascorbate. Biochim. Biophys. Acta 47 (1961) 288–297.
3.  Suzuki, K., Kawada, M. and Shimazono, N. Soluble lactonase. Identity of lactonase I and aldonolactonase with gluconolactonase. J. Biochem. (Tokyo) 49 (1961) 448–449.
[EC 3.1.1.17 created 1961 (EC 3.1.1.18 created 1961, incorporated 1982)]
 
 
EC 3.1.1.18      
Deleted entry:  aldonolactonase. Now included with EC 3.1.1.17 gluconolactonase
[EC 3.1.1.18 created 1961, deleted 1982]
 
 
EC 3.1.1.19     
Accepted name: uronolactonase
Reaction: D-glucurono-6,2-lactone + H2O = D-glucuronate
Other name(s): glucuronolactonase
Systematic name: D-glucurono-6,2-lactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-93-8
References:
1.  Winkelman, J. and Lehninger, A.L. Aldono- and uronolactonase of animal tissues. J. Biol. Chem. 233 (1958) 794–799. [PMID: 13587494]
[EC 3.1.1.19 created 1961]
 
 
EC 3.1.1.20     
Accepted name: tannase
Reaction: digallate + H2O = 2 gallate
Glossary: gallate = 3,4,5-trihydroxybenzoate
digallate = 3,4-dihydroxy-5-(3,4,5-trihydroxybenzoyloxy)benzoate
Other name(s): tannase S; tannin acetylhydrolase
Systematic name: tannin acylhydrolase
Comments: Also hydrolyses ester links in other tannins.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-71-2
References:
1.  Dyckerhoff, H. and Armbruster, R. Zur Kenntnis der Tannase. Hoppe-Seyler's Z. Physiol. Chem. 219 (1933) 38–56.
[EC 3.1.1.20 created 1961]
 
 
EC 3.1.1.21      
Deleted entry: retinyl-palmitate esterase. Now known to be catalysed by EC 3.1.1.1, carboxylesterase and EC 3.1.1.3, triacylglycerol lipase.
[EC 3.1.1.21 created 1972, deleted 2011]
 
 
EC 3.1.1.22     
Accepted name: hydroxybutyrate-dimer hydrolase
Reaction: (R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O = 2 (R)-3-hydroxybutanoate
Other name(s): D-(-)-3-hydroxybutyrate-dimer hydrolase
Systematic name: (R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37278-37-8
References:
1.  Delafield, F.P., Cooksey, K.E. and Doudoroff, M. β-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. J. Biol. Chem. 240 (1965) 4023–4028. [PMID: 4954074]
[EC 3.1.1.22 created 1972]
 
 
EC 3.1.1.23     
Accepted name: acylglycerol lipase
Reaction: Hydrolyses glycerol monoesters of long-chain fatty acids
Other name(s): monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase
Systematic name: glycerol-ester acylhydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9040-75-9
References:
1.  Mentlein, R., Heiland, S. and Heymann, E. Simultaneous purification and comparative characterization of six serine hydrolases from rat liver microsomes. Arch. Biochem. Biophys. 200 (1980) 547–559. [DOI] [PMID: 6776896]
2.  Pope, J.L., McPherson, J.C. and Tidwell, H.C. A study of a monoglyceride-hydrolyzing enzyme of intestinal mucosa. J. Biol. Chem. 241 (1966) 2306–2310. [PMID: 5916497]
[EC 3.1.1.23 created 1972]
 
 
EC 3.1.1.24     
Accepted name: 3-oxoadipate enol-lactonase
Reaction: 3-oxoadipate enol-lactone + H2O = 3-oxoadipate
For diagram of benzoate metabolism, click here
Other name(s): carboxymethylbutenolide lactonase; β-ketoadipic enol-lactone hydrolase; 3-ketoadipate enol-lactonase; 3-oxoadipic enol-lactone hydrolase; β-ketoadipate enol-lactone hydrolase
Systematic name: 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
Comments: The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9031-04-3
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway. J. Biol. Chem. 241 (1966) 3787–3794. [PMID: 5916392]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 3.1.1.24 created 1961 as EC 3.1.1.16, part transferred 1972 to EC 3.1.1.24]
 
 
EC 3.1.1.25     
Accepted name: 1,4-lactonase
Reaction: a 1,4-lactone + H2O = a 4-hydroxyacid
Other name(s): γ-lactonase
Systematic name: 1,4-lactone hydroxyacylhydrolase
Comments: The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37278-38-9
References:
1.  Fishbein, W.N. and Bessman, S.P. Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase. J. Biol. Chem. 241 (1966) 4835–4841. [PMID: 4958984]
2.  Fishbein, W.N. and Bessman, S.P. Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. II. Metal ion effects, kinetics, and equilibria. J. Biol. Chem. 241 (1966) 4842–4847. [PMID: 4958985]
[EC 3.1.1.25 created 1972, modified 1981]
 
 
EC 3.1.1.26     
Accepted name: galactolipase
Reaction: 1,2-diacyl-3-β-D-galactosyl-sn-glycerol + 2 H2O = 3-β-D-galactosyl-sn-glycerol + 2 carboxylates
Other name(s): galactolipid lipase; polygalactolipase; galactolipid acylhydrolase
Systematic name: 1,2-diacyl-3-β-D-galactosyl-sn-glycerol acylhydrolase
Comments: Also acts on 2,3-di-O-acyl-1-O-(6-O-α-D-galactosyl-β-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37278-40-3
References:
1.  Helmsing, P.J. Purification and properties of galactolipase. Biochim. Biophys. Acta 178 (1969) 519–533. [DOI] [PMID: 5784904]
2.  Hirayama, O., Matsuda, H., Takeda, H., Maenaka, K. and Takatsuka, H. Purification and properties of a lipid acyl-hydrolase from potato tubers. Biochim. Biophys. Acta 384 (1975) 127–137. [DOI] [PMID: 236765]
[EC 3.1.1.26 created 1972]
 
 
EC 3.1.1.27     
Accepted name: 4-pyridoxolactonase
Reaction: 4-pyridoxolactone + H2O = 4-pyridoxate
For diagram of pyridoxal catabolism, click here
Systematic name: 4-pyridoxolactone lactonohydrolase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37278-41-4
References:
1.  Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585–2589. [PMID: 4306030]
[EC 3.1.1.27 created 1972]
 
 
EC 3.1.1.28     
Accepted name: acylcarnitine hydrolase
Reaction: O-acylcarnitine + H2O = a fatty acid + L-carnitine
Other name(s): high activity acylcarnitine hydrolase; HACH; carnitine ester hydrolase; palmitoylcarnitine hydrolase; palmitoyl-L-carnitine hydrolase; long-chain acyl-L-carnitine hydrolase; palmitoyl carnitine hydrolase
Systematic name: O-acylcarnitine acylhydrolase
Comments: Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37278-42-5
References:
1.  Mahadevan, S. and Sauer, F. Carnitine ester hydrolase of rat liver. J. Biol. Chem. 244 (1969) 4448–4453. [PMID: 5806585]
2.  Mentlein, R., Reuter, G. and Heymann, E. Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function. Arch. Biochem. Biophys. 240 (1985) 801–810. [DOI] [PMID: 4026306]
[EC 3.1.1.28 created 1972]
 
 
EC 3.1.1.29     
Accepted name: peptidyl-tRNA hydrolase
Reaction: N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
Other name(s): aminoacyl-transfer ribonucleate hydrolase; N-substituted aminoacyl transfer RNA hydrolase; aminoacyl-tRNA hydrolase; PTH1 (gene name); PTH2 (gene name); pth (gene name); spoVC (gene name); PTRH1 (gene name); PTRH2 (gene name)
Systematic name: peptidyl-tRNA peptidylhydrolase
Comments: The enzyme acts on premature protein synthesis products that dissociate from stalled ribosomes, cleaving the peptidyl chains and restoring functionality to the tRNA. In most organisms mutants with limited Pth activity accumulate peptidyl-tRNAs, reducing the availability of uncharged tRNAs below the limit that is necessary for protein synthesis and impairing cell growth. Two distinct classes of the enzyme, Pth and Pth2, have been identified. While most enzymes can recognize and cleave N-acylated aminoacyl-tRNAs, they are not able to act on N-formyl-methionyl-tRNA.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9054-98-2
References:
1.  Cuzin, F., Kretchmer, N., Greenberg, R.E., Hurwitz, R. and Chapeville, F. Enzymatic hydrolysis of N-substituted aminoacyl-tRNA. Proc. Natl. Acad. Sci. USA 58 (1967) 2079–2086. [DOI] [PMID: 4866985]
2.  Kossel, H. and RajBhandary, U.L. Studies on polynucleotides. LXXXVI. Enzymic hydrolysis of N-acylaminoacyl-transfer RNA. J. Mol. Biol. 35 (1968) 539–560. [DOI] [PMID: 4877004]
3.  Jost, J.-P. and Bock, R.M. Enzymatic hydrolysis of N-substituted aminoacyl transfer ribonucleic acid in yeast. J. Biol. Chem. 244 (1969) 5866–5873. [DOI] [PMID: 4981785]
4.  Menninger, J.R. Accumulation of peptidyl tRNA is lethal to Escherichia coli. J. Bacteriol. 137 (1979) 694–696. [DOI] [PMID: 368041]
5.  Dutka, S., Meinnel, T., Lazennec, C., Mechulam, Y. and Blanquet, S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucleic Acids Res. 21 (1993) 4025–4030. [DOI] [PMID: 7690473]
6.  Menez, J., Buckingham, R.H., de Zamaroczy, M. and Campelli, C.K. Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded by spoVC, is essential to vegetative growth, whereas the homologous enzyme in Saccharomyces cerevisiae is dispensable. Mol. Microbiol. 45 (2002) 123–129. [DOI] [PMID: 12100553]
7.  Rosas-Sandoval, G., Ambrogelly, A., Rinehart, J., Wei, D., Cruz-Vera, L.R., Graham, D.E., Stetter, K.O., Guarneros, G. and Soll, D. Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast. Proc. Natl. Acad. Sci. USA 99 (2002) 16707–16712. [DOI] [PMID: 12475929]
8.  De Pereda, J.M., Waas, W.F., Jan, Y., Ruoslahti, E., Schimmel, P. and Pascual, J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279 (2004) 8111–8115. [DOI] [PMID: 14660562]
[EC 3.1.1.29 created 1972, modified 2023]
 
 
EC 3.1.1.30     
Accepted name: D-arabinonolactonase
Reaction: D-arabinono-1,4-lactone + H2O = D-arabinonate
For diagram of D-arabinose catabolism, click here
Systematic name: D-arabinono-1,4-lactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37278-44-7
References:
1.  Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophilla. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180–185. [PMID: 13475218]
[EC 3.1.1.30 created 1972]
 
 
EC 3.1.1.31     
Accepted name: 6-phosphogluconolactonase
Reaction: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
For diagram of the early stages of the pentose-phosphate pathway, click here
Other name(s): phosphogluconolactonase; 6-PGL
Systematic name: 6-phospho-D-glucono-1,5-lactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37278-45-8
References:
1.  Kawada, M., Kagawa, Y., Takiguchi, H. and Shimazono, N. Purification of 6-phosphogluconolactonase from rat liver and yeast; its separation from gluconolactonase. Biochim. Biophys. Acta 57 (1962) 404–407. [DOI] [PMID: 14454532]
2.  Miclet, E., Stoven, V., Michels, P.A., Opperdoes, F.R., Lallemand, J.-Y. and Duffieux, F. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276 (2001) 34840–34846. [DOI] [PMID: 11457850]
[EC 3.1.1.31 created 1972]
 
 
EC 3.1.1.32     
Accepted name: phospholipase A1
Reaction: phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
Systematic name: phosphatidylcholine 1-acylhydrolase
Comments: This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9043-29-2
References:
1.  Gatt, S. Purification and properties of phospholipase A-1 from rat and calf brain. Biochim. Biophys. Acta 159 (1968) 304–316. [DOI] [PMID: 5657461]
2.  Scandella, C.J. and Kornberg, A. A membrane-bound phospholipase A1 purified from Escherichia coli. Biochemistry 10 (1971) 4447–4456. [PMID: 4946924]
3.  van den Bosch, H. Intracellular phospholipases A. Biochim. Biophys. Acta 604 (1980) 191–246. [DOI] [PMID: 6252969]
4.  van den Bosch, H., Aarsman, A.J. and van Deenen, L.L.M. Isolation and properties of a phospholipase A1 activity from beef pancreas. Biochim. Biophys. Acta 348 (1974) 197–209. [DOI] [PMID: 4858811]
[EC 3.1.1.32 created 1972, modified 1976]
 
 
EC 3.1.1.33     
Accepted name: 6-acetylglucose deacetylase
Reaction: 6-acetyl-D-glucose + H2O = D-glucose + acetate
Other name(s): 6-O-acetylglucose deacetylase
Systematic name: 6-acetyl-D-glucose acetylhydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 37278-46-9
References:
1.  Duff, R.B. and Webley, D.M. Metabolism of 6-O-acetyl-D-glucopyranose and other monoacetyl-sugars by strains of Bacillus megaterium and other soil organisms. Biochem. J. 70 (1958) 520–528. [PMID: 13596370]
[EC 3.1.1.33 created 1972]
 
 
EC 3.1.1.34     
Accepted name: lipoprotein lipase
Reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate
Other name(s): clearing factor lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; hepatic triacylglycerol lipase; LIPC (gene name); LPL (gene name); triacylglycero-protein acylhydrolase
Systematic name: triacylglycerol acylhydrolase (lipoprotein-dependent)
Comments: Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride → 1,2-diglyceride → 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9004-02-8
References:
1.  Egelrud, T. and Olivecrona, T. Purified bovine milk (lipoprotein) lipase: activity against lipid substrates in the absence of exogenous serum factors. Biochim. Biophys. Acta 306 (1973) 115–127. [DOI] [PMID: 4703566]
2.  Fielding, C.J. Human lipoprotein lipase. I. Purification and substrate specificity. Biochim. Biophys. Acta 206 (1970) 109–117. [DOI] [PMID: 5441398]
3.  Greten, H., Levy, R.I., Fales, H. and Fredrickson, D.S. Hydrolysis of diglyceride and glyceryl monoester diethers with lipoprotein lipase. Biochim. Biophys. Acta 210 (1970) 39–45. [DOI] [PMID: 5466051]
4.  Morley, N. and Kuksis, A. Positional specificity of lipoprotein lipase. J. Biol. Chem. 247 (1972) 6389–6393. [PMID: 5076762]
5.  Nilsson-Ehle, P., Belfrage, P. and Borgström, B. Purified human lipoprotein lipase: positional specificity. Biochim. Biophys. Acta 248 (1971) 114–120. [DOI] [PMID: 5168777]
6.  Santamarina-Fojo, S., Gonzalez-Navarro, H., Freeman, L., Wagner, E. and Nong, Z. Hepatic lipase, lipoprotein metabolism, and atherogenesis. Arterioscler Thromb Vasc Biol 24 (2004) 1750–1754. [PMID: 15284087]
[EC 3.1.1.34 created 1972, modified 1976]
 
 
EC 3.1.1.35     
Accepted name: dihydrocoumarin hydrolase
Reaction: dihydrocoumarin + H2O = melilotate
Systematic name: dihydrocoumarin lactonohydrolase
Comments: Also hydrolyses some other benzenoid 1,4-lactones.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37278-47-0
References:
1.  Kosuge, T. and Conn, E.E. The metabolism of aromatic compounds in higher plants. V. Purification and properties of dihydrocoumarin hydrolase of Melilotus alba. J. Biol. Chem. 237 (1962) 1653–1656. [PMID: 14458747]
[EC 3.1.1.35 created 1972]
 
 
EC 3.1.1.36     
Accepted name: limonin-D-ring-lactonase
Reaction: limonoate D-ring-lactone + H2O = limonoate
Other name(s): limonin-D-ring-lactone hydrolase; limonin lactone hydrolase
Systematic name: limonoate-D-ring-lactone lactonohydrolase
Comments: Limonoate is a triterpenoid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-17-8
References:
1.  Maier, V.P., Hasegawa, S. and Hera, E. Limonin D-ring-lactone hydrolase. A new enzyme from Citrus seeds. Phytochemistry 8 (1969) 405–407.
[EC 3.1.1.36 created 1972]
 
 
EC 3.1.1.37     
Accepted name: steroid-lactonase
Reaction: testololactone + H2O = testolate
Glossary: testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13-lactone
testolate = 13-hydroxy-3-oxo-13,17-secoandrost-4-en-17-oate
Systematic name: testololactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-08-7
References:
1.  Holmlund, C.E. and Blank, R.H. Preparation and properties of a steroid lactonase. Arch. Biochem. Biophys. 109 (1965) 29–35. [DOI] [PMID: 14281950]
[EC 3.1.1.37 created 1972]
 
 
EC 3.1.1.38     
Accepted name: triacetate-lactonase
Reaction: triacetate lactone + H2O = triacetate
Other name(s): triacetic lactone hydrolase; triacetic acid lactone hydrolase; TAL hydrolase; triacetate lactone hydrolase
Systematic name: triacetolactone lactonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9023-02-3
References:
1.  Kato, S., Ueda, H., Nonomura, S. and Tatsumi, C. [Degradation of dehydroacetic acid by microorganisms. III. Properties of triacetic acid lactone hydrolase.] Nippon Nogei Kagaku Kaishi 42 (1968) 596–600. (in Japanese)
[EC 3.1.1.38 created 1972]
 
 
EC 3.1.1.39     
Accepted name: actinomycin lactonase
Reaction: actinomycin + H2O = actinomycinic monolactone
Systematic name: actinomycin lactonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-09-8
References:
1.  Hou, C.T. and Perlman, D. Microbial transformations of peptide antibiotics. V. Purification and properties of the actinomycin lactonase from Actinoplanes missouriensis. J. Biol. Chem. 245 (1970) 1289–1295. [PMID: 4191854]
[EC 3.1.1.39 created 1972]
 
 
EC 3.1.1.40     
Accepted name: orsellinate-depside hydrolase
Reaction: orsellinate depside + H2O = 2 orsellinate
Glossary: orsellinate = 2,4-dihydroxy-6-methylbenzoate
Other name(s): lecanorate hydrolase
Systematic name: orsellinate-depside hydrolase
Comments: The enzyme will only hydrolyse those substrates based on the 2,4-dihydroxy-6-methylbenzoate structure that also have a free hydroxy group ortho to the depside linkage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-12-1
References:
1.  Schultz, J. and Mosbach, K. Studies on lichen enzymes. Purification and properties of an orsellinate depside hydrolase obtained from Lasallia pustulata. Eur. J. Biochem. 22 (1971) 153–157. [DOI] [PMID: 5116606]
[EC 3.1.1.40 created 1976]
 
 
EC 3.1.1.41     
Accepted name: cephalosporin-C deacetylase
Reaction: cephalosporin C + H2O = deacetylcephalosporin C + acetate
For diagram of cephalosporin biosynthesis, click here
Other name(s): cephalosporin C acetyl-hydrolase; cephalosporin C acetylase; cephalosporin acetylesterase; cephalosporin C acetylesterase; cephalosporin C acetyl-esterase; cephalosporin C deacetylase
Systematic name: cephalosporin-C acetylhydrolase
Comments: Hydrolyses the acetyl ester bond on the 10-position of the antibiotic cephalosporin C.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 52227-71-1
References:
1.  Fujisawa, Y., Shirafuji, H., Kida, M. and Nara, K. New findings on cephalosporin C biosynthesis. Nat. New Biol. 246 (1973) 154–155. [PMID: 4519146]
[EC 3.1.1.41 created 1976]
 
 
EC 3.1.1.42     
Accepted name: chlorogenate hydrolase
Reaction: chlorogenate + H2O = caffeate + quinate
Other name(s): chlorogenase; chlorogenic acid esterase
Systematic name: chlorogenate hydrolase
Comments: Also acts, more slowly, on isochlorogenate. No other substrates are known.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74082-59-0
References:
1.  Schöbel, B. and Pollmann, W. Isolation and characterization of a chlorogenic acid esterase from Aspergillus niger. Z. Naturforsch. C: Biosci. 35 (1980) 209–212. [PMID: 7385941]
2.  Schöbel, B. and Pollmann, W. Weitere Charakterisierung einer Chlorogensäure - Hydrolase aus Aspergillus niger. Z. Naturforsch. C: Biosci. 35 (1980) 699–701. [PMID: 7445677]
[EC 3.1.1.42 created 1981]
 
 
EC 3.1.1.43     
Accepted name: α-amino-acid esterase
Reaction: an α-amino acid ester + H2O = an α-amino acid + an alcohol
Other name(s): α-amino acid ester hydrolase
Systematic name: α-amino-acid-ester aminoacylhydrolase
Comments: Also catalyses α-aminoacyl transfer to a number of amine nucleophiles.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 74506-40-4
References:
1.  Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A. Purification of an α-amino acid ester hydrolase from Xanthomonas citri. Agric. Biol. Chem. 44 (1980) 1069–1074.
2.  Kato, K., Kawahara, K., Takahashi, T. and Kakinuma, A. Substrate specificity of an α-amino acid ester hydrolase from Xanthomonas citri. Agric. Biol. Chem. 44 (1980) 1075–1081.
3.  Takahashi, T., Yamazaki, Y. and Kato, K. Substrate specificity of an α-amino acid ester hydrolase produced by Acetobacter turbidans A. T.C.C. 9325. Biochem. J. 137 (1974) 497–503. [PMID: 4424889]
[EC 3.1.1.43 created 1983]
 
 
EC 3.1.1.44     
Accepted name: 4-methyloxaloacetate esterase
Reaction: oxaloacetate 4-methyl ester + H2O = oxaloacetate + methanol
Systematic name: oxaloacetate-4-methyl-ester oxaloacetohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74812-46-7
References:
1.  Donnelly, M.I. and Dagley, S. Production of methanol from aromatic acids by Pseudomonas putida. J. Bacteriol. 142 (1980) 916–924. [PMID: 7380811]
[EC 3.1.1.44 created 1983]
 
 
EC 3.1.1.45     
Accepted name: carboxymethylenebutenolidase
Reaction: 4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate
Other name(s): maleylacetate enol-lactonase; dienelactone hydrolase; carboxymethylene butenolide hydrolase
Systematic name: 4-carboxymethylenebut-2-en-4-olide lactonohydrolase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 76689-22-0
References:
1.  Schmidt, E. and Knackmuss, H.-J. Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid. Biochem. J. 192 (1980) 339–347. [PMID: 7305906]
[EC 3.1.1.45 created 1983]
 
 
EC 3.1.1.46     
Accepted name: deoxylimonate A-ring-lactonase
Reaction: deoxylimonate + H2O = deoxylimononic acid D-ring-lactone
Systematic name: deoxylimonate A-ring-lactonohydrolase
Comments: The enzyme opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the D-ring-lactone intact.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75788-82-8
References:
1.  Hasegawa, H., Bennett, R.D. and Verdon, C.P. Metabolism of limonoids via a deoxylimonoid pathway in Citrus. Phytochemistry 19 (1980) 1445–1447.
[EC 3.1.1.46 created 1983]
 
 
EC 3.1.1.47     
Accepted name: 1-alkyl-2-acetylglycerophosphocholine esterase
Reaction: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Other name(s): 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase; alkylacetyl-GPC:acetylhydrolase
Systematic name: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 76901-00-3
References:
1.  Blank, M.L., Lee, T.-C., Fitzgerald, V. and Snyder, F. A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a hypotensive and platelet-activating lipid). J. Biol. Chem. 256 (1981) 175–178. [PMID: 7451433]
[EC 3.1.1.47 created 1984]
 
 
EC 3.1.1.48     
Accepted name: fusarinine-C ornithinesterase
Reaction: N5-acyl-L-ornithine ester + H2O = N5-acyl-L-ornithine + an alcohol
Other name(s): ornithine esterase; 5-N-acyl-L-ornithine-ester hydrolase
Systematic name: N5-acyl-L-ornithine-ester hydrolase
Comments: Hydrolyses the three ornithine ester bonds in fusarinine C. Also acts on N5-dinitrophenyl-L-ornithine methyl ester.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-10-0
References:
1.  Emery, T. Fungal ornithine esterases: relationship to iron transport. Biochemistry 15 (1976) 2723–2728. [PMID: 949472]
[EC 3.1.1.48 created 1984]
 
 
EC 3.1.1.49     
Accepted name: sinapine esterase
Reaction: sinapoylcholine + H2O = sinapate + choline
Other name(s): aromatic choline esterase
Systematic name: sinapoylcholine sinapohydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 72506-67-3
References:
1.  Nurmann, G. and Strack, D. Sinapine esterase. 1. Characterization of sinapine esterase from cotyledons of Raphanus sativus. Z. Naturforsch. C: Biosci. 34 (1979) 715–720.
[EC 3.1.1.49 created 1984]
 
 
EC 3.1.1.50     
Accepted name: wax-ester hydrolase
Reaction: a wax ester + H2O = a long-chain alcohol + a long-chain carboxylate
Other name(s): jojoba wax esterase; WEH
Systematic name: wax-ester acylhydrolase
Comments: Also acts on long-chain acylglycerol, but not diacyl- or triacylglycerols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66625-78-3
References:
1.  Huang, A.H.C., Moreau, R.A. and Liu, K.D.F. Development and properties of a wax ester hydrolase in the cotyledons of jojoba seedlings. Plant Physiol. 61 (1978) 339–341. [PMID: 16660288]
2.  Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
[EC 3.1.1.50 created 1984]
 
 


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