Continued from EC 3.1.1.51 to EC 3.1.1.122
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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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, Metacyc, 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, Metacyc, 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]
[EC 3.1.2.15 Deleted entry: This activity is covered by EC 3.4.19.12, ubiquitinyl hydrolase 1 (EC 3.1.2.15 created 1986, deleted 2014)]
Accepted name: citrate lyase deacetylase
Reaction: acetyl-[citrate (pro-3S)-lyase] + H2O = holo-[citrate (pro-3S)-lyase] + acetate
Other name(s): [citrate-(pro-3S)-lyase] thiolesterase; acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase; citrate lyase deacetylase; [citrate-(pro-3S)-lyase](acetyl-form) hydrolase
Systematic name: acetyl-[citrate-(pro-3S)-lyase] hydrolase
Comments: In the proteobacterium Rubrivivax gelatinosus, this enzyme modulates the activity of EC 4.1.3.6, citrate (pro-3S)-lyase, by converting it from its active acetyl form into its inactive thiol form by removal of its acetyl groups [2]. The activity of citrate-lyase deacetylase is itself inhibited by L-glutamate [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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, Metacyc, 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]
[EC 3.1.2.26 Transferred entry: bile-acid-CoA hydrolase, now classified as EC 2.8.3.25, bile acid CoA transferase. (EC 3.1.2.26 created 2005, deleted 2016)]
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, Metacyc, 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]
Accepted name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Reaction: 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA
For diagram of reaction click here.
Systematic name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Comments: This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Muller, W. and Leistner, E. 1,4-Naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis. Phytochemistry 15 (1976) 407-410.
2. Eichinger, D., Bacher, A., Zenk, M.H. and Eisenreich, W. Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum. J. Am. Chem. Soc. 121 (1999) 7469-7475.
3. Widhalm, J.R., van Oostende, C., Furt, F. and Basset, G.J. A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. Proc. Natl. Acad. Sci. USA 106 (2009) 5599-5603. [PMID: 19321747]
4. Chen, M., Ma, X., Chen, X., Jiang, M., Song, H. and Guo, Z. Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. J. Bacteriol. 195 (2013) 2768-2775. [PMID: 23564174]
Accepted name: fluoroacetyl-CoA thioesterase
Reaction: fluoroacetyl-CoA + H2O = fluoroacetate + CoA
Systematic name: fluoroacetyl-CoA hydrolase
Comments: Fluoroacetate is extremely toxic. It reacts with CoA to form fluoroacetyl-CoA, which substitutes for acetyl CoA and reacts with EC 2.3.3.1 (citrate synthase) to produce fluorocitrate, a metabolite of which binds very tightly to EC 4.2.1.3 (aconitase) and halts the TCA cycle. This enzyme hydrolyses fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance on the organisms that produce it. It has been described in the poisonous plant Dichapetalum cymosum and the bacterium Streptomyces cattleya, both of which are fluoroacetate producers.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Meyer, J.J.M., Grobbelaar, N., Vleggaar, R. and Louw, A.I. Fluoroacetyl-coenzyme-A hydrolase-like activity in Dichapetalum cymosum. J. Plant Physiol. 139 (1992) 369-372.
2. Huang, F., Haydock, S.F., Spiteller, D., Mironenko, T., Li, T.L., O'Hagan, D., Leadlay, P.F. and Spencer, J.B. The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A. Chem. Biol. 13 (2006) 475-484. [PMID: 16720268]
3. Dias, M.V., Huang, F., Chirgadze, D.Y., Tosin, M., Spiteller, D., Dry, E.F., Leadlay, P.F., Spencer, J.B. and Blundell, T.L. Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK. J. Biol. Chem. 285 (2010) 22495-22504. [PMID: 20430898]
Accepted name: (3S)-malyl-CoA thioesterase
Reaction: (S)-malyl-CoA + H2O = (S)-malate + CoA
Glossary: (S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): mcl2 (gene name)
Systematic name: (S)-malyl-CoA hydrolase
Comments: Stimulated by Mg2+ or Mn2+. The enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Erb, T.J., Frerichs-Revermann, L., Fuchs, G. and Alber, B.E. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192 (2010) 1249-1258. [PMID: 20047909]
Accepted name: dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase
Reaction: dihydromonacolin L-[lovastatin nonaketide synthase] + H2O = holo-[lovastatin nonaketide synthase] + dihydromonacolin L acid
For diagram of reaction click here.
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovG
Systematic name: dihydromonacolin L-[lovastatin nonaketide synthase] hydrolase
Comments: Dihydromonacolin L acid is synthesized while bound to an acyl-carrier protein domain of the lovastatin nonaketide synthase (EC 2.3.1.161). Since that enzyme lacks a thioesterase domain, release of the dihydromonacolin L acid moiety from the polyketide synthase requires this dedicated enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Xu, W., Chooi, Y.H., Choi, J.W., Li, S., Vederas, J.C., Da Silva, N.A. and Tang, Y. LovG: the thioesterase required for dihydromonacolin L release and lovastatin nonaketide synthase turnover in lovastatin biosynthesis. Angew. Chem. Int. Ed. Engl. 52 (2013) 6472-6475. [PMID: 23653178]
Accepted name: 2-aminobenzoylacetyl-CoA thioesterase
Reaction: 2-aminobenzoylacetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA
Other name(s): pqsE (gene name)
Systematic name: (2-aminobenzoyl)acetyl-CoA hydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Yu, S., Jensen, V., Seeliger, J., Feldmann, I., Weber, S., Schleicher, E., Haussler, S. and Blankenfeldt, W. Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry 48 (2009) 10298-10307. [PMID: 19788310]
2. Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611-618. [PMID: 25960261]
Accepted name: betainyl-CoA thioesterase
Reaction: betaine-CoA + H2O = glycine betaine + CoA
Glossary: betaine-CoA = glycinebetainyl-CoA = betainyl-CoA = N,N,N-trimethylglycyl-CoA
Other name(s): cdhB (gene name)
Systematic name: betaine-CoA hydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in an L-carnitine degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wargo, M.J. and Hogan, D.A. Identification of genes required for Pseudomonas aeruginosa carnitine catabolism. Microbiology (Reading) 155 (2009) 2411-2419. [PMID: 19406895]
2. Bastard, K., Smith, A.A., Vergne-Vaxelaire, C., Perret, A., Zaparucha, A., De Melo-Minardi, R., Mariage, A., Boutard, M., Debard, A., Lechaplais, C., Pelle, C., Pellouin, V., Perchat, N., Petit, J.L., Kreimeyer, A., Medigue, C., Weissenbach, J., Artiguenave, F., De Berardinis, V., Vallenet, D. and Salanoubat, M. Revealing the hidden functional diversity of an enzyme family. Nat. Chem. Biol. 10 (2014) 42-49. [PMID: 24240508]