Continued from EC 3.1.1.51 to EC 3.1.1.82
Accepted name: acetyl-CoA hydrolase
Reaction: acetyl-CoA + H2O = CoA + acetate
Other name(s): acetyl-CoA deacylase; acetyl-CoA acylase; acetyl coenzyme A hydrolase; acetyl coenzyme A deacylase; acetyl coenzyme A acylase; acetyl-CoA thiol esterase
Systematic name: acetyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9027-54-7
References:
1. Gergely, J., Hele, P. and Ramakrishnan, C.V. Succinyl and acetyl coenzyme A deacylases. J. Biol. Chem. 198 (1952) 323-334.
Accepted name: palmitoyl-CoA hydrolase
Reaction: palmitoyl-CoA + H2O = CoA + palmitate
Other name(s): long-chain fatty-acyl-CoA hydrolase; palmitoyl coenzyme A hydrolase; palmitoyl thioesterase; palmitoyl coenzyme A hydrolase; palmitoyl-CoA deacylase; palmityl thioesterase; palmityl-CoA deacylase; fatty acyl thioesterase I; palmityl thioesterase I
Systematic name: palmitoyl-CoA hydrolase
Comments: Also hydrolyses CoA thioesters of other long-chain fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-87-0
References:
1. Barnes, E.M., Jr. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J. Biol. Chem. 243 (1968) 2955-2962. [PMID: 4871199]
2. Berge, R.K. and Farstad, M. Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria. Methods Enzymol. 71 (1981) 234-242. [PMID: 6116156]
3. Miyazawa, S., Furuta, S. and Hashimoto, T. Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators. Eur. J. Biochem. 117 (1981) 425-430. [PMID: 6115749]
4. Srere, P.A., Seubert, W. and Lynen, F. Palmityl coenzyme A deacylase. Biochim. Biophys. Acta 33 (1959) 313-319.
5. Yabusaki, K.K. and Ballou, C.E. Long-chain fatty acyl-CoA thioesterases from Mycobacterium smegmatis. Methods Enzymol. 71 (1981) 242-246.
Accepted name: succinyl-CoA hydrolase
Reaction: succinyl-CoA + H2O = CoA + succinate
Other name(s): succinyl-CoA acylase; succinyl coenzyme A hydrolase; succinyl coenzyme A deacylase
Systematic name: succinyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-86-9
References:
1. Gergely, J., Hele, P. and Ramakrishnan, C.V. Succinyl and acetyl coenzyme A deacylases. J. Biol. Chem. 198 (1952) 323-334.
Accepted name: 3-hydroxyisobutyryl-CoA hydrolase
Reaction: 3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate
Other name(s): 3-hydroxy-isobutyryl CoA hydrolase; HIB CoA deacylase
Systematic name: 3-hydroxy-2-methylpropanoyl-CoA hydrolase
Comments: Also hydrolyses 3-hydroxypropanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-88-1
References:
1. Rendina, G. and Coon, M.J. Enzymatic hydrolysis of the coenzyme A thiol esters of β-hydroxypropionic and β-hydroxyisobutyric acids. J. Biol. Chem. 225 (1957) 523-534.
Accepted name: hydroxymethylglutaryl-CoA hydrolase
Reaction: (S)-3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate
For diagram click here.
Other name(s): β-hydroxy-β-methylglutaryl coenzyme A hydrolase; β-hydroxy-β-methylglutaryl coenzyme A deacylase; hydroxymethylglutaryl coenzyme A hydrolase; hydroxymethylglutaryl coenzyme A deacylase; 3-hydroxy-3-methylglutaryl-CoA hydrolase
Systematic name: (S)-3-hydroxy-3-methylglutaryl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-89-2
References:
1. Dekker, E.E., Schlesinger, M.J. and Coon, M.J. β-Hydroxy-β-methylglutaryl coenzyme A deacetylase. J. Biol. Chem. 233 (1958) 434-438.
Accepted name: hydroxyacylglutathione hydrolase
Reaction: S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
Other name(s): glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase
Systematic name: S-(2-hydroxyacyl)glutathione hydrolase
Comments: Also hydrolyses S-acetoacetylglutathione, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9025-90-5
References:
1. Racker, E. Spectrophotometric measurements of the metabolic formation and degradation of thiol esters and enediol compounds. Biochim. Biophys. Acta 9 (1952) 577-579.
2. Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938-3943. [PMID: 4200890]
3. Uotila, L. Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12 (1973) 3944-3951. [PMID: 4745654]
Accepted name: glutathione thiolesterase
Reaction: S-acylglutathione + H2O = glutathione + a carboxylate
Other name(s): citryl-glutathione thioesterhydrolase
Systematic name: S-acylglutathione hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-99-4
References:
1. Kielley, W.W. and Bradley, L.B. Glutathione thiolesterase. J. Biol. Chem. 206 (1954) 327-338.
[EC 3.1.2.8 Deleted entry: S-acetoacylglutathione hydrolase. Now included with EC 3.1.2.6 hydroxyacylglutathione hydrolase (EC 3.1.2.8 created 1961, deleted 1978)]
[EC 3.1.2.9 Deleted entry: S-acetoacetylhydrolipoate hydrolase (EC 3.1.2.9 created 1961, deleted 1964)]
Accepted name: formyl-CoA hydrolase
Reaction: formyl-CoA + H2O = CoA + formate
Other name(s): formyl coenzyme A hydrolase
Systematic name: formyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9025-91-6
References:
1. Sly, W.S. and Stadtman, E.R. Formate metabolism. I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl phosphate in Clostridium kluyveri. J. Biol. Chem. 238 (1963) 2632-2638.
Accepted name: acetoacetyl-CoA hydrolase
Reaction: acetoacetyl-CoA + H2O = CoA + acetoacetate
For diagram click here.
Other name(s): acetoacetyl coenzyme A hydrolase; acetoacetyl CoA deacylase; acetoacetyl coenzyme A deacylase
Systematic name: acetoacetyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37288-10-1
References:
1. Aragón, J.J. and Lowenstein, J.M. A survey of enzymes which generate or use acetoacetyl thioesters in rat liver. J. Biol. Chem. 258 (1983) 4725-4733. [PMID: 6131897]
2. Drummond, G.I. and Stern, J.R. Enzymes of ketone body metabolism. II. Properties of an acetoacetate-synthesizing enzyme prepared from ox liver. J. Biol. Chem. 235 (1960) 318-325.
Accepted name: S-formylglutathione hydrolase
Reaction: S-formylglutathione + H2O = glutathione + formate
Systematic name: S-formylglutathione hydrolase
Comments: Also hydrolyses S-acetylglutathione, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, CAS registry number: 83380-83-0
References:
1. Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938-3943. [PMID: 4200890]
2. Uotila, L. and Koivusalo, M. Purification and properties of S-formylglutathione hydrolase from human liver. J. Biol. Chem. 249 (1974) 7664-7672. [PMID: 4436331]
3. Harms, N., Ras, J., Reijnders, W.N., van Spanning, R.J. and Stouthamer, A.H. S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? J. Bacteriol. 178 (1996) 6296-6299. [PMID: 8892832]
Accepted name: S-succinylglutathione hydrolase
Reaction: S-succinylglutathione + H2O = glutathione + succinate
Systematic name: S-succinylglutathione hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 50812-22-1
References:
1. Uotila, L. Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938-3943. [PMID: 4200890]
2. Uotila, L. Purification and properties of S-succinylglutathione hydrolase from human liver. J. Biol. Chem. 254 (1979) 7024-7029. [PMID: 457667]
Accepted name: oleoyl-[acyl-carrier-protein] hydrolase
Reaction: an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate
Other name(s): acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase
Systematic name: oleoyl-[acyl-carrier protein] hydrolase
Comments: Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 68009-83-6
References:
1. Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382-391. [PMID: 30409]
2. Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins. Arch. Biochem. Biophys. 172 (1976) 110-116. [PMID: 3134]
Accepted name: ubiquitin thiolesterase
Reaction: ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol
Other name(s): ubiquitin carboxy-terminal esterase; isopeptidase; isopeptidase T; ubiquitin C-terminal hydrolase; ubiquitin carboxy-terminal hydrolase; ubiquitin-C-terminal-thiolester hydrolase
Systematic name: ubiquitin-C-terminal-thioester hydrolase
Comments: Acts on esters formed between thiols such as dithiothreitol or glutathione and the C-terminal glycine residue of the polypeptide ubiquitin. Also acts on AMP-ubiquitin. May be the same as EC 3.4.19.12, ubiquitinyl hydrolase 1.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 86480-67-3
References:
1. Rose, I.A. and Warms, J.V.B. An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes. Biochemistry 22 (1983) 4234-4237. [PMID: 6313036]
Accepted name: citrate lyase deacetylase
Reaction: [citrate (pro-3S)-lyase](acetyl form) + H2O = [citrate (pro-3S)-lyase](thiol form) + acetate
Other name(s): [citrate-(pro-3S)-lyase] thiolesterase
Systematic name: [citrate-(pro-3S)-lyase](acetyl-form) hydrolase
Comments: Hydrolysis inactivates EC 4.1.3.6 citrate (pro-3S)-lyase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 58319-93-0
References:
1. Giffhorn, F., Rode, H., Kuhn, A. and Gottschalk, G. Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate. Eur. J. Biochem. 111 (1980) 461-471. [PMID: 7460909]
Accepted name: (S)-methylmalonyl-CoA hydrolase
Reaction: (S)-methylmalonyl-CoA + H2O = methylmalonate + CoA
Other name(s): D-methylmalonyl-coenzyme A hydrolase
Systematic name: (S)-methylmalonyl-CoA hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 87928-03-8
References:
1. Kovachy, R.J., Copley, S.D. and Allen, R.H. Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase. J. Biol. Chem. 258 (1983) 11415-11421. [PMID: 6885824]
Accepted name: ADP-dependent short-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): short-chain acyl coenzyme A hydrolase; propionyl coenzyme A hydrolase; propionyl-CoA hydrolase; propionyl-CoA thioesterase; short-chain acyl-CoA hydrolase; short-chain acyl-CoA thioesterase
Systematic name: ADP-dependent-short-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 117698-16-5
References:
1. Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564-13571. [PMID: 2901416]
2. Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13-19. [PMID: 2570608]
Accepted name: ADP-dependent medium-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): medium-chain acyl coenzyme A hydrolase; medium-chain acyl-CoA hydrolase; medium-chain acyl-thioester hydrolase; medium-chain hydrolase; myristoyl-CoA thioesterase
Systematic name: ADP-dependent-medium-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 63363-75-7
References:
1. Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564-13571. [PMID: 2901416]
Accepted name: acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): acyl coenzyme A thioesterase; acyl-CoA thioesterase; acyl coenzyme A hydrolase; thioesterase B; thioesterase II; acyl-CoA thioesterase
Systematic name: acyl-CoA hydrolase
Comments: Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37270-64-7
References:
1. Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria in the rat.Biochim. Biophys. Acta 1005 (1989) 13-19. [PMID: 2570608]
Accepted name: dodecanoyl-[acyl-carrier protein] hydrolase
Reaction: a dodecanoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + dodecanoate
Other name(s): lauryl-acyl-carrier-protein hydrolase; dodecanoyl-acyl-carrier-protein hydrolase; dodecyl-acyl-carrier protein hydrolase
Systematic name: dodecanoyl-[acyl-carrier protein] hydrolase
Comments: acts on the acyl-carrier-protein thioester of C12 and, with a much lower activity, C14 fatty acids. The derivative of oleic acid is hydrolysed very slowly (cf. EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 137903-37-8
References:
1. Pollard, M.R., Anderson, L., Fan, C., Hawkins, D.J., Davies, H.M. A specific acyl-ACP thioesterase implicated in medium-chain fatty acid production in immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 284 (1991) 306-312. [PMID: 1989513]
2. Davies, H.M., Anderson, L., Fan, C., Hawkins, D.J. Developmental induction, purification, and further characterization of 12:0-ACP thioesterase from immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 290 (1991) 37-45. [PMID: 1898097]
Accepted name: palmitoyl[protein] hydrolase
Reaction: palmitoyl[protein] + H2O = palmitate + protein
Other name(s): palmitoyl-protein thioesterase; palmitoyl-(protein) hydrolase
Systematic name: palmitoyl[protein] hydrolase
Comments: specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 150605-49-5
References:
1. Camp, L.A., Hofmann, S.L. Assay and isolation of palmitoyl-protein thioesterase from bovine brain using palmitoylated H-Ras as substrate. Methods Enzymol. 250 (1995) 336-347. [PMID: 7651163]
2. Schriner, J.E., Yi, W., Hofmann, S.L. cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics, 34 (1996) 317-322. [PMID: 8786130]
3. Verkruyse, L.A., Hofmann, S.L. Lysosomal targeting of palmitoyl-protein thioesterase. J. Biol. Chem. 271 (1996) 15831-15836. [PMID: 8663305]
Accepted name: 4-hydroxybenzoyl-CoA thioesterase
Reaction: 4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA
Systematic name: 4-hydroxybenzoyl-CoA hydrolase
Comments: this enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, PDB, CAS registry number: 141583-19-9
References:
1.Chang, K.H., Liang, P.H., Beck, W., Scholten, J.D., Dunaway-Mariano, D. Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3. Biochemistry 31 (1992) 5605-5610. [PMID: 1610806]
2.Dunaway-Mariano, D., Babbitt, P.C. On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway. Biodegradation 5 (1994) 259-276. [PMID: 7765837]
[EC 3.1.2.24 Transferred entry: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase, the enzyme was incorrectly classified as a thioester hydrolase when the bond broken is a C-S bond, which is not an ester. Now EC 3.13.1.3, 2'-hydroxybiphenyl-2-sulfinate desulfinase (EC 3.1.2.24 created 2000, deleted 2005)]
Accepted name: phenylacetyl-CoA hydrolase
Reaction: phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA
For diagram of reaction click here.
Systematic name: phenylglyoxylyl-CoA hydrolase
Comments: This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 57219-72-4
References:
1. Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507-515. [PMID: 10336636]
2. Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509-516. [PMID: 9575237]
Accepted name: bile-acid-CoA hydrolase
Reaction: deoxycholoyl-CoA + H2O = CoA + deoxycholate
Systematic name: deoxycholoyl-CoA hydrolase
Comments: Choloyl-CoA, 3-dehydrocholoyl-CoA and chenodeoxycholoyl-CoA can also act as substrates, but acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA and phenylacetyl-CoA cannot.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 220983-07-3
References:
1. Ye, H.Q., Mallonee, D.H., Wells, J.E., Bjorkhem, I. and Hylemon, P.B. The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase. J. Lipid Res. 40 (1999) 17-23. [PMID: 9869646]
Accepted name: choloyl-CoA hydrolase
Reaction: choloyl-CoA + H2O = cholate + CoA
For diagram click here.
Other name(s): PTE-2 (ambiguous); choloyl-coenzyme A thioesterase; chenodeoxycholoyl-coenzyme A thioesterase; peroxisomal acyl-CoA thioesterase 2
Systematic name: choloyl-CoA hydrolase
Comments: Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoAs, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoAs, all of which are present in peroxisomes. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Hunt, M.C., Solaas, K., Kase, B.F. and Alexson, S.E. Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. J. Biol. Chem. 277 (2002) 1128-1138. [PMID: 11673457]
2. Solaas, K., Sletta, R.J., Soreide, O. and Kase, B.F. Presence of choloyl- and chenodeoxycholoyl-coenzyme A thioesterase activity in human liver. Scand. J. Clin. Lab. Invest. 60 (2000) 91-102. [PMID: 10817395]
3. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]