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acetyl-CoA]; citrate oxaloacetate-lyase, CoA-acetylating; citrate synthase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme; oxaloacetate transacetase; oxalacetic transacetase
Accepted name: citrate (Si)-synthase
Reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA
For diagram of reaction click here (stereochemistry) (another example).
Other name(s): (R)-citric synthase; citrate condensing enzyme; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-acetyl-CoA]; citrate oxaloacetate-lyase, CoA-acetylating; citrate synthase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme; oxaloacetate transacetase; oxalacetic transacetase
Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-S)-carboxymethyl forming]
Comments: The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, citrate (Re)-synthase, which is found in some anaerobes.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-96-7
References:
1. Gottschalk, G. Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici. Eur. J. Biochem. 7 (1969) 301-306. [PMID: 4974734]
2. Ochoa, S., Stern, J.R. and Schneider, M.C. Enzymatic synthesis of citric acid. II. Crystalline condensing enzyme. J. Biol. Chem. 193 (1951) 691-702.
3. Stern, J.R. Oxalacetate transacetase (condensing enzyme, citrogenase), in Boyer, P,D., Lardy, H and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 5, Academic Press, New York, 1961, pp. 367-380.
4. Rault-Leonardon, M., Atkinson, M.A., Slaughter, C.A., Moomaw, C.R. and Srere, P.A. Azotobacter vinelandii citrate synthase. Biochemistry 34 (1995) 257-263. [PMID: 7819205]
5. Muir, J.M., Russell, R.J., Hough, D.W. and Danson, M.J. Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus. Prot. Eng. 8 (1995) 583-592.
6. Russell, R.J., Ferguson, J.M., Hough, D.W., Danson, M.J. and Taylor, G.L. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution. Biochemistry 36 (1997) 9983-9994. [PMID: 9254593]
Accepted name: decylcitrate synthase
Reaction: lauroyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA
For diagram click here.
Other name(s): 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating)
Systematic name: dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9068-72-8
References:
1. Måhlén, A. and Gatenbeck, S. A metabolic variation in Penicillium spiculisporum Lehman. II. Purification and some properties of the enzyme synthesizing (–)-decylcitric acid. Acta Chem. Scand. 22 (1968) 2617-2623. [PMID: 5719165]
2. Måhlén, A. Properties of 2-decylcitrate synthase from Penicillium spiculisporum Lehman. Eur. J. Biochem. 22 (1971) 104-114. [PMID: 5099208]
Accepted name: citrate (Re)-synthase
Reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA
For diagram click here.
Other name(s): (R)-citrate synthase; Re-citrate-synthase; citrate oxaloacetate-lyase [(pro-3R)-CH2COO-acetyl-CoA]
Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-R)-carboxymethyl-forming]
Comments: This enzyme is inactivated by oxygen and is found in some anaerobes. Its stereospecificity is opposite to that of EC 2.3.3.1, citrate (Si)-synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9077-70-7
References:
1. Dittbrenner, S., Chowdhury, A.A. and Gottschalk, G. The stereospecificity of the (R)-citrates synthase in the presence of p-chloromercuribenzoate. Biochem. Biophys. Res. Commun. 36 (1969) 802-808. [PMID: 5808294]
2. Gottschalk, G. Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici. Eur. J. Biochem. 7 (1969) 301-306. [PMID: 4974734]
3. Gottschalk, G. and Barker, H.A. Synthesis of glutamate and citrate by Clostridium kluyveri. A new type of citrate synthase. Biochemistry 5 (1966) 1125-1133. [PMID: 5958189]
Accepted name: decylhomocitrate synthase
Reaction: dodecanoyl-CoA + H2O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA
For diagram click here.
Other name(s): 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating)
Systematic name: dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)
Comments: Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51845-40-0
References:
1. Måhlén, A. Purification and some properties of 2-decylhomocitrate synthase from Penicillium spiculisporum. Eur. J. Biochem. 38 (1973) 32-39. [PMID: 4774124]
2. Brandäge, S., Dahlman, O., Lindqvist, B., Måhlén, A. and Mörch, L. Absolute configuration and enantiospecific synthesis of spiculisporic acid. Acta Chem. Scand. 38B (1984) 837-844.
Accepted name: 2-methylcitrate synthase
Reaction: propanoyl-CoA + H2O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
For diagram click here.
Glossary: 2-methylcitrate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate.
Other name(s): 2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase
Systematic name: propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming)
Comments: The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme has been separated from EC 2.3.3.1 citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 57827-78-8
References:
1. Uchiyama, H. and Tabuchi, T. Properties of methylcitrate synthase from Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1411-1418.
2. Textor, S., Wendisch, V.F., De Graaf, A.A., Muller, U., Linder, M.I., Linder, D. and Buckel, W. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168 (1997) 428-436. [PMID: 9325432]
3. Horswill, A.R. and Escalante-Semerena, J.C. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181 (1999) 5615-5623. [PMID: 10482501]
4. van Rooyen, J.P.G., Mienie, L.J., Erasmus, E., De Wet, W.J., Ketting, D., Duran, M. and Wadman, S.K. Identification of the stereoisomeric configurations of methylcitric acid produced by Si-citrate synthase and methylcitrate synthase using capillary gas chromatography-mass spectrometry. J. Inherit. Metab. Dis. 17 (1994) 738-747. [PMID: 7707698]
Accepted name: 2-ethylmalate synthase
Reaction: acetyl-CoA + H2O + 2-oxobutanoate = (R)-2-ethylmalate + CoA
For diagram click here.
Other name(s): (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating); 2-ethylmalate-3-hydroxybutanedioate synthase; propylmalate synthase; propylmalic synthase
Systematic name: acetyl-CoA:2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Comments: Also acts on (R)-2-(n-propyl)-malate. Formerly wrongly included with EC 2.3.3.7 3-ethylmalate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-01-5
References:
1. Strassman, M. and Ceci, L.N. A study of acetyl-CoA condensation with α-keto acids. Arch. Biochem. Biophys. 119 (1967) 420-428. [PMID: 6052435]
Accepted name: 3-ethylmalate synthase
Reaction: butanoyl-CoA + H2O + glyoxylate = 3-ethylmalate + CoA
For diagram click here.
Other name(s): 2-ethyl-3-hydroxybutanedioate synthase; 3-ethylmalate glyoxylate-lyase (CoA-butanoylating)
Systematic name: butanoyl-CoA:glyoxylate C-butanoyltransferase (thioester-hydrolysing, 1-carboxypropyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-01-5
References:
1. Ramasarma, T. and Giri, K.V. Phosphoglucose isomerase of green gram (Phaseolus radiatus). Arch. Biochem. Biophys. 62 (1956) 91-96.
Accepted name: ATP citrate synthase
Reaction: ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Other name(s): ATP-citric lyase; ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-acetyl-CoA] (ATP-dephosphorylating); acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating); adenosine triphosphate citrate lyase; citrate cleavage enzyme; citrate-ATP lyase; citric cleavage enzyme; ATP citrate (pro-S)-lyase
Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]
Comments: The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate—CoA ligase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-95-6
References:
1. Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645-650. [PMID: 6749502]
2. Srere, P.A. and Lipmann, F. An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A. J. Am. Chem. Soc. 75 (1953) 4874 only.
Accepted name: malate synthase
Reaction: acetyl-CoA + H2O + glyoxylate = S)-malate + CoA
For diagram of reaction click here.
Other name(s): L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme
Systematic name: acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9013-48-3
References:
1. Dixon, G.H., Kornberg, H.L. and Lund, P. Purification and properties of malate synthetase. Biochim. Biophys. Acta 41 (1960) 217-233. [PMID: 13816984]
Accepted name: hydroxymethylglutaryl-CoA synthase
Reaction: acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
For diagram click here.
Other name(s): (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating); 3-hydroxy-3-methylglutaryl CoA synthetase; 3-hydroxy-3-methylglutaryl coenzyme A synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthetase; 3-hydroxy-3-methylglutaryl-CoA synthase; 3-hydroxy-3-methylglutaryl-coenzyme A synthase; β-hydroxy-β-methylglutaryl-CoA synthase; HMG-CoA synthase; acetoacetyl coenzyme A transacetase; hydroxymethylglutaryl coenzyme A synthase; hydroxymethylglutaryl coenzyme A-condensing enzyme
Systematic name: acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-44-5
References:
1. Rudney, H. The biosynthesis of β-hydroxy-β-methylglutaric acid. J. Biol. Chem. 227 (1957) 363-377.
Accepted name: 2-hydroxyglutarate synthase
Reaction: propanoyl-CoA + H2O + glyoxylate = 2-hydroxyglutarate + CoA
Other name(s): 2-hydroxyglutaratic synthetase; 2-hydroxyglutaric synthetase; α-hydroxyglutarate synthase; hydroxyglutarate synthase; 2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating)
Systematic name: propanoyl-CoA:glyoxylate C-propanoyltransferase (thioester-hydrolysing, 2-carboxyethyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-02-6
References:
1. Reeves, H.C. and Ajl, S.J. α-Hydroxyglutaric acid synthetase. J. Bacteriol. 84 (1962) 186-187.
Accepted name: 3-propylmalate synthase
Reaction: pentanoyl-CoA + H2O + glyoxylate = 3-propylmalate + CoA
For diagram click here.
Other name(s): 3-(n-propyl)-malate synthase; 3-propylmalate glyoxylate-lyase (CoA-pentanoylating); β-n-propylmalate synthase; n-propylmalate synthase
Systematic name: pentanoyl-CoA:glyoxylate C-pentanoyltransferase (thioester-hydrolysing, 1-carboxybutyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-62-3
References:
1. Imai, K., Reeves, H.C. and Ajl, S.J. n-Propylmalate synthetase. J. Biol. Chem. 238 (1963) 3193-3198.
Accepted name: 2-isopropylmalate synthase
Reaction: acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA
For diagram of reaction click here.
Other name(s): 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating); α-isopropylmalate synthetase; α-isopropylmalate synthase; α-isopropylmalic synthetase; isopropylmalate synthase; isopropylmalate synthetase
Systematic name: acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Comments: Requires K+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-98-2
References:
1. Kohlhaw, G., Leary, T.R. and Umbarger, H.E. α-Isopropylmalate synthase from Salmonella typhimurium. Purification and properties. J. Biol. Chem. 244 (1969) 2218-2225. [PMID: 4976555]
2. Webster, R.E. and Gross, S.R. The α-isopropylmalate synthetase of Neurospora. I. The kinetics and end product control of α-isopropylmalate synthetase function. Biochemistry 4 (1965) 2309-2327.
3. Cole, F.E., Kalyanpur, M. G. and Stevens, C. M. Absolute configuration of α-isopropylmalate and the mechanism of its conversion to β-isopropylmalate in the biosynthesis of leucine. Biochemistry 12 (1973) 3346-3350. [PMID: 4270046]
Accepted name: homocitrate synthase
Reaction: acetyl-CoA + H2O + 2-oxoglutarate = (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
For diagram click here, another example.
Glossary: (R)-homocitrate = (R)-2-hydroxybutane-1,2,4-tricarboxylate
Other name(s): 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating); acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; homocitrate synthetase; HCS
Systematic name: acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming)
Comments: Belongs in the α-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with oxaloacetate as substrate, but more slowly [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-60-9
References:
1. Strassman, M. and Ceci, L.N. Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis. Biochem. Biophys. Res. Commun. 14 (1964) 262-267. [PMID: 5836514]
2. Wulandari, A.P., Miyazaki, J., Kobashi, N., Nishiyama, M., Hoshino, T. and Yamane, H. Characterization of bacterial homocitrate synthase involved in lysine biosynthesis. FEBS Lett. 522 (2002) 35-40. [PMID: 12095615]
3. Andi, B., West, A.H. and Cook, P.F. Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. Biochemistry 43 (2004) 11790-11795. [PMID: 15362863]
Accepted name: sulfoacetaldehyde acetyltransferase
Reaction: acetyl phosphate + sulfite = 2-sulfoacetaldehyde + phosphate
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): Xsc
Systematic name: acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2-oxoethyl-forming)
Comments: The reaction occurs in the reverse direction to that shown above. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56941-15-2
References:
1. Ruff, J, Denger, K. and Cook, A.M. Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. Biochem. J. 369 (2003) 275-285. [PMID: 12358600]