EC |
2.3.3.1 |
Accepted name: |
citrate (Si)-synthase |
Reaction: |
acetyl-CoA + H2O + oxaloacetate = citrate + CoA |
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For diagram of the citric acid cycle, click here and for diagram of the glyoxylate cycle, click here |
Other name(s): |
(R)-citric synthase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-→acetyl-CoA] |
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. Citrate synthase for which the stereospecificity with respect to C-2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase (unknown stereospecificity). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-96-7 |
References: |
1. |
Lenz, H., Buckel, W., Wunderwald, P., Biedermann, G., Buschmeier, V., Eggerer, H., Cornforth, J.W., Redmond, J.W. and Mallaby, R. Stereochemistry of si-citrate synthase and ATP-citrate-lyase reactions. Eur. J. Biochem. 24 (1971) 207–215. [DOI] [PMID: 5157292] |
2. |
Karpusas, M., Branchaud, B. and Remington, S.J. Proposed mechanism for the condensation reaction of citrate synthase: 1.9-Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A. Biochemistry 29 (1990) 2213–2219. [PMID: 2337600] |
3. |
van Rooyen, J.P., 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] |
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[EC 2.3.3.1 created 1961 as EC 4.1.3.7, transferred 2002 to EC 2.3.3.1, modified 2014] |
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EC |
2.3.3.10 |
Accepted name: |
hydroxymethylglutaryl-CoA synthase |
Reaction: |
acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA |
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For diagram of the mevalonate-biosynthesis pathway, 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. [PMID: 13449080] |
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[EC 2.3.3.10 created 1961 as EC 4.1.3.5, transferred 2002 to EC 2.3.3.10] |
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EC |
2.3.3.11 |
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. [PMID: 14491016] |
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[EC 2.3.3.11 created 1965 as EC 4.1.3.9, transferred 2002 to EC 2.3.3.11] |
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EC |
2.3.3.12 |
Accepted name: |
3-propylmalate synthase |
Reaction: |
pentanoyl-CoA + H2O + glyoxylate = 3-propylmalate + CoA |
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For diagram of reaction, 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. [PMID: 14085361] |
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[EC 2.3.3.12 created 1972 as EC 4.1.3.11, transferred 2002 to EC 2.3.3.12] |
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EC |
2.3.3.13 |
Accepted name: |
2-isopropylmalate synthase |
Reaction: |
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA |
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For diagram of leucine-biosynthesis pathway, 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] |
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[EC 2.3.3.13 created 1972 as EC 4.1.3.12, transferred 2002 to EC 2.3.3.13] |
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EC |
2.3.3.14 |
Accepted name: |
homocitrate synthase |
Reaction: |
acetyl-CoA + H2O + 2-oxoglutarate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA |
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For diagram of L-Lysine synthesis, click here |
Glossary: |
(R)-homocitrate = (2R)-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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15362863] |
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[EC 2.3.3.14 created 1972 as EC 4.1.3.21, transferred 2002 to EC 2.3.3.14] |
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EC |
2.3.3.15 |
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. [DOI] [PMID: 12358600] |
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[EC 2.3.3.15 created 2003] |
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EC |
2.3.3.16 |
Accepted name: |
citrate synthase (unknown stereospecificity) |
Reaction: |
acetyl-CoA + H2O + oxaloacetate = citrate + CoA |
Other name(s): |
citrate condensing enzyme; CoA-acetylating citrate oxaloacetate-lyase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme (ambiguous); oxaloacetate transacetase; oxalacetic transacetase |
Systematic name: |
acetyl-CoA:oxaloacetate C-acetyltransferase (thioester-hydrolysing) |
Comments: |
This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C-2 of oxaloacetate has not been established [cf. EC 2.3.3.1, citrate (Si)-synthase and EC 2.3.3.3, citrate (Re)-synthase]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Lohlein-Werhahn, G., Goepfert, P. and Eggerer, H. Purification and properties of an archaebacterial enzyme: citrate synthase from Sulfolobus solfataricus. Biol. Chem. Hoppe Seyler 369 (1988) 109–113. [PMID: 3130075] |
2. |
Sievers, M., Stockli, M. and Teuber, M. Purification and properties of citrate synthase from Acetobacter europaeus. FEMS Microbiol. Lett. 146 (1997) 53–58. [DOI] [PMID: 8997706] |
3. |
Belova, L.L., Sokolov, A.P., Morgunov, I.G. and Trotsenko YuA. Purification and characterization of citrate synthase from Methylobacterium extorquens—a methylotrophic producer of polyhydroxybutyrate. Biochemistry (Mosc.) 62 (1997) 71–76. [PMID: 9113733] |
4. |
Lee, S., Park, C. and Yim, J. Characterization of citrate synthase purified from Drosophila melanogaster. Mol. Cells 7 (1997) 599–604. [PMID: 9387145] |
5. |
Maurus, R., Nguyen, N.T., Stokell, D.J., Ayed, A., Hultin, P.G., Duckworth, H.W. and Brayer, G.D. Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases. Biochemistry 42 (2003) 5555–5565. [DOI] [PMID: 12741811] |
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[EC 2.3.3.16 created 2014] |
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EC |
2.3.3.17 |
Accepted name: |
methylthioalkylmalate synthase |
Reaction: |
an ω-(methylsulfanyl)-2-oxoalkanoate + acetyl-CoA + H2O = a 2-[ω-(methylsulfanyl)alkyl]malate + CoA |
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For diagram of L-Homomethionine biosynthesis, click here |
Other name(s): |
MAM1 (gene name); MAM3 (gene name); acetyl-CoA:ω-(methylthio)-2-oxoalkanoate C-acetyltransferase |
Systematic name: |
acetyl-CoA:ω-(methylsulfanyl)-2-oxoalkanoate C-acetyltransferase |
Comments: |
The enzyme, characterized from the plant Arabidopsis thaliana, is involved in the L-methionine side-chain elongation pathway, forming substrates for the biosynthesis of aliphatic glucosinolates. Two forms are known - MAM1 catalyses only only the first two rounds of methionine chain elongation, while MAM3 catalyses all six cycles, up to formation of L-hexahomomethionine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Textor, S., Bartram, S., Kroymann, J., Falk, K.L., Hick, A., Pickett, J.A. and Gershenzon, J. Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle. Planta 218 (2004) 1026–1035. [DOI] [PMID: 14740211] |
2. |
Textor, S., de Kraker, J.W., Hause, B., Gershenzon, J. and Tokuhisa, J.G. MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis. Plant Physiol. 144 (2007) 60–71. [DOI] [PMID: 17369439] |
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[EC 2.3.3.17 created 2016] |
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EC |
2.3.3.18 |
Accepted name: |
2-phosphinomethylmalate synthase |
Reaction: |
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate = phosphinomethylmalate + CoA |
Other name(s): |
pmmS (gene name) |
Systematic name: |
acetyl-CoA:phosphinopyruvate C-acetyltransferase (thioester-hydrolysing, phosphinomethylmalate-forming) |
Comments: |
The enzyme, characterized from the bacterium Streptomyces hygroscopicus, participates in the pathway for bialaphos biosynthesis. It requires a divalent metal ion and can also act on oxaloacetate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Shimotohno, K.W., Seto, H., Otake, N., Imai, S. and Murakami, T. Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and characterization of 2-phosphinomethylmalic acid synthase from Streptomyces hygroscopicus SF-1293. J. Antibiot. (Tokyo) 41 (1988) 1057–1065. [PMID: 3170341] |
2. |
Shimotohno, K.W., Imai, S., Murakami, T. and Seto, H. Purification and characterization of citrate synthase from Streptomyces hygroscopicus SF-1293 and comparison of its properties with those of 2-phosphinomethylmalic acid synthase. Agric. Biol. Chem. 54 (1990) 463–470. [PMID: 1368511] |
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[EC 2.3.3.18 created 2017] |
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EC |
2.3.3.19 |
Accepted name: |
2-phosphonomethylmalate synthase |
Reaction: |
acetyl-CoA + H2O + 3-phosphonopyruvate = (R)-2-(phosphonomethyl)malate + CoA |
Other name(s): |
2-phosphinomethylmalic acid synthase; PMM synthase |
Systematic name: |
acetyl-CoA:3-phosphonopyruvate C-acetyltransferase |
Comments: |
The enzyme, isolated from several Streptomyces species, participate in the biosynthesis of certain phosphonate antibiotics. The enzyme is analogous to EC 2.3.3.1 (Si)-citrate synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Shimotohno, K., Seto, H., Otake, N., Imai, S. and Satoh, A. Studies on the biosynthesis of bialaphos (SE-1293). 7. The absolute configuration of 2-phosphinomethylmalic acid, a biosynthetic intermediate of bialaphos. J. Antibiot. (Tokyo) 39 (1986) 1356–1359. [PMID: 3781934] |
2. |
Shimotohno, K.W., Seto, H., Otake, N., Imai, S. and Murakami, T. Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and characterization of 2-phosphinomethylmalic acid synthase from Streptomyces hygroscopicus SF-1293. J. Antibiot. (Tokyo) 41 (1988) 1057–1065. [PMID: 3170341] |
3. |
Eliot, A.C., Griffin, B.M., Thomas, P.M., Johannes, T.W., Kelleher, N.L., Zhao, H. and Metcalf, W.W. Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098. Chem. Biol. 15 (2008) 765–770. [DOI] [PMID: 18721747] |
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[EC 2.3.3.19 created 2017] |
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