Enzyme Nomenclature

EC 3.1

Acting on Ester Bonds

Sections

EC 3.1.1 Carboxylic Ester Hydrolases
EC 3.1.2 Thiolester Hydrolases
EC 3.1.3 Phosphoric Monoester Hydrolases
EC 3.1.4 Phosphoric Diester Hydrolases
EC 3.1.5 Triphosphoric Monoester Hydrolases
EC 3.1.6 Sulfuric Ester Hydrolases
EC 3.1.7 Diphosphoric Monoester Hydrolases
EC 3.1.8 Phosphoric Triester Hydrolases
EC 3.1.11 Exodeoxyribonucleases Producing 5'-Phosphomonoesters
EC 3.1.12 Exodeoxyribonucleases Producing 3'-Phosphomonoesters
EC 3.1.13 Exoribonucleases Producing 5'-Phosphomonoesters
EC 3.1.14 Exoribonucleases Producing 3'-Phosphomonoesters
EC 3.1.15 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters
EC 3.1.16 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters
EC 3.1.21 Endodeoxyribonucleases Producing 5'-Phosphomonoesters
EC 3.1.22 Endodeoxyribonucleases Producing 3'-Phosphomonoesters
EC 3.1.25 Site-Specific Endodeoxyribonucleases Specific for Altered Bases
EC 3.1.26 Endoribonucleases Producing 5'-Phosphomonoesters
EC 3.1.27 Endoribonucleases Producing 3'-Phosphomonoesters
EC 3.1.30 Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters
EC 3.1.31 Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters


3.1.1 Carboxylic Ester Hydrolases

See separate file for EC 3.1.1.51 to EC 3.1.1.102.

Contents

EC 3.1.1.1 carboxylesterase
EC 3.1.1.2 arylesterase
EC 3.1.1.3 triacylglycerol lipase
EC 3.1.1.4 phospholipase A2
EC 3.1.1.5 lysophospholipase
EC 3.1.1.6 acetylesterase
EC 3.1.1.7 acetylcholinesterase
EC 3.1.1.8 cholinesterase
EC 3.1.1.9 deleted
EC 3.1.1.10 tropinesterase
EC 3.1.1.11 pectinesterase
EC 3.1.1.12 deleted
EC 3.1.1.13 sterol esterase
EC 3.1.1.14 chlorophyllase
EC 3.1.1.15 L-arabinonolactonase
EC 3.1.1.16 deleted, mixture of EC 5.3.3.4 and EC 3.1.1.24
EC 3.1.1.17 gluconolactonase
EC 3.1.1.18 deleted, included in EC 3.1.1.17
EC 3.1.1.19 uronolactonase
EC 3.1.1.20 tannase
EC 3.1.1.21 deleted, catalysed by EC 3.1.1.1 and EC 3.1.1.3
EC 3.1.1.22 hydroxybutyrate-dimer hydrolase
EC 3.1.1.23 acylglycerol lipase
EC 3.1.1.24 3-oxoadipate enol-lactonase
EC 3.1.1.25 1,4-lactonase
EC 3.1.1.26 galactolipase
EC 3.1.1.27 4-pyridoxolactonase
EC 3.1.1.28 acylcarnitine hydrolase
EC 3.1.1.29 aminoacyl-tRNA hydrolase
EC 3.1.1.30 D-arabinonolactonase
EC 3.1.1.31 6-phosphogluconolactonase
EC 3.1.1.32 phospholipase A1
EC 3.1.1.33 6-acetylglucose deacetylase
EC 3.1.1.34 lipoprotein lipase
EC 3.1.1.35 dihydrocoumarin hydrolase
EC 3.1.1.36 limonin-D-ring-lactonase
EC 3.1.1.37 steroid-lactonase
EC 3.1.1.38 triacetate-lactonase
EC 3.1.1.39 actinomycin lactonase
EC 3.1.1.40 orsellinate-depside hydrolase
EC 3.1.1.41 cephalosporin-C deacetylase
EC 3.1.1.42 chlorogenate hydrolase
EC 3.1.1.43 α-amino-acid esterase
EC 3.1.1.44 4-methyloxaloacetate esterase
EC 3.1.1.45 carboxymethylenebutenolidase
EC 3.1.1.46 deoxylimonate A-ring-lactonase
EC 3.1.1.47 1-alkyl-2-acetylglycerophosphocholine esterase
EC 3.1.1.48 fusarinine-C ornithinesterase
EC 3.1.1.49 sinapine esterase
EC 3.1.1.50 wax-ester hydrolase

See the following file for:

EC 3.1.1.51 to EC 3.1.1.102

Entries

EC 3.1.1.1

Accepted name: carboxylesterase

Reaction: A carboxylic ester + H2O = an alcohol + a carboxylate

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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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. [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. [PMID: 5353595]

4. Burch, J. The purification and properties of horse liver esterase. Biochem. J. 58 (1954) 415-426.

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. [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; paraoxonase; 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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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 of swine. I. 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. [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. [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. (Eds.) 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. [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. [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

Other name(s): lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; 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

Systematic name: triacylglycerol acylhydrolase

Comments: The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolysed.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-62-1

References:

1. Korn, E.D. and Quigley, T.W. Lipoprotein lipase of chicken adipose tissue. J. Biol. Chem. 226 (1957) 833-839.

2. Lynn, W.S. and Perryman, N.C. Properties and purification of adipose tissue lipase. J. Biol. Chem. 235 (1960) 1912-1916.

3. Sarda, L. and Desnuelle, P. Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta 30 (1958) 513-521.

4. 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.

5. Singer, T.P. and Hofstee, B.H.J. Studies on wheat germ lipase. II. Kinetics. Arch. Biochem. 18 (1948) 245-259.

[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, 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.

2. Fraenkel-Conrat, H. and Fraenkel-Conrat, J. Inactivation of crotoxin by group-specific reagents. Biochim. Biophys. Acta 5 (1950) 98-104.

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.

4. Moore, J.H. and Williams, D.L. Some observations on the specificity of phospholipase A. Biochim. Biophys. Acta 84 (1964) 41-54.

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.

6. van den Bosch, H. Intracellular phospholipases A. Biochim. Biophys. Acta 604 (1980) 191-246. [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, 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.

4. Fairbairn, D. The preparation and properties of a lysophospholipase from Penicillium notatum. J. Biol. Chem. 173 (1948) 705-714.

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. [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. [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. [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. [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 reaction 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, EXPASY, KEGG, UM-BBD, Metacyc, PDB, UM-BBD, 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.

2. Bergmann, F. and Rimon, S. Fractionation of C-esterase from the hog's kidney extract. Biochem. J. 77 (1960) 209-214.

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.

[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, 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. 52 (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.

3. Cilliv, G. and Ozand, P.T. Human erythrocyte acetylcholinesterase purification, properties and kinetic behavior. Biochim. Biophys. Acta 284 (1972) 136-156. [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. [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.

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.

[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, 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. 52 (1948).

2. Augustinsson, K.-B. and Olsson, B. Esterases in the milk and blood of swine. I. Substrate specificity and electrophoresis studies. Biochem. J. 71 (1959) 477-484.

3. Koelle, G.B. Cholinesterases of the tissues and sera of rabbits. Biochem. J. 53 (1953) 217-226.

4. Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259-339.

5. Sawyer, C.H. Hydrolysis of choline esters by liver. Science 101 (1945) 385-386.

6. Strelitz, F. Studies on cholinesterase. 4. Purification of pseudo-cholinesterase from horse serum. Biochem. J. 38 (1944) 86-88.

[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, EXPASY, KEGG, Metacyc, UM-BBD, 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, 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.

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.

[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, 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 click here or 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, KEGG, Metacyc, 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. [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. [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 reaction click here.

Systematic name: L-arabinono-1,4-lactone lactonohydrolase

Links to other databases: BRENDA, EXPASY, 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.

[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 D-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 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 as EC 3.1.1.18, aldonolactonase.

Links to other databases: BRENDA, EXPASY, 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.

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, 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.

[EC 3.1.1.19 created 1961]

EC 3.1.1.20

Accepted name: tannase

Reaction: digallate + H2O = 2 gallate

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, KEGG, Metacyc, 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, 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, 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. [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.

[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 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, 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, KEGG, Metacyc, 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, 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. [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. [PMID: 236765]

[EC 3.1.1.26 created 1972]

EC 3.1.1.27

Accepted name: 4-pyridoxolactonase

Reaction: 4-pyridoxolactone + H2O = 4-pyridoxate

Systematic name: 4-pyridoxolactone lactonohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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, KEGG, Metacyc, UM-BBD, 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. [PMID: 4026306]

[EC 3.1.1.28 created 1972]

EC 3.1.1.29

Accepted name: aminoacyl-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; peptidyl-tRNA hydrolase

Systematic name: aminoacyl-tRNA aminoacylhydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-98-2

References:

1. 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. [PMID: 4981785]

[EC 3.1.1.29 created 1972]

EC 3.1.1.30

Accepted name: D-arabinonolactonase

Reaction: D-arabinono-1,4-lactone + H2O = D-arabinonate

Systematic name: D-arabinono-1,4-lactone lactonohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-44-7

References:

1. Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophila. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180-185.

[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 click here.

Other name(s): phosphogluconolactonase; 6-PGL

Systematic name: 6-phospho-D-glucono-1,5-lactone lactonohydrolase

Links to other databases: BRENDA, EXPASY, 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.

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. [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, 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. [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. [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. [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, 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.

[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; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor

Systematic name: triacylglycero-protein acylhydrolase

Comments: Hydrolyses triacylglycerols in chylomicrons and low-density lipoproteins. Also hydrolyses diacylglycerol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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. [PMID: 4703566]

2. Fielding, C.J. Human lipoprotein lipase. I. Purification and substrate specificity. Biochim. Biophys. Acta 206 (1970) 109-117. [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. [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. [PMID: 5168777]

[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, KEGG, Metacyc, 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.

[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.

[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. [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

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, 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, 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, EXPASY, KEGG, UM-BBD, Metacyc, PDB, UM-BBD, 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, 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

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, 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.

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]


Continued with EC 3.1.1.51 to EC 3.1.1.102
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