The Enzyme Database

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EC 2.3.3.1     
Accepted name: citrate (Si)-synthase
Reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA
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]
[EC 2.3.3.1 created 1961 as EC 4.1.3.7, transferred 2002 to EC 2.3.3.1, modified 2014]
 
 
EC 2.3.3.10     
Accepted name: hydroxymethylglutaryl-CoA synthase
Reaction: acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
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]
[EC 2.3.3.10 created 1961 as EC 4.1.3.5, transferred 2002 to EC 2.3.3.10]
 
 
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]
[EC 2.3.3.11 created 1965 as EC 4.1.3.9, transferred 2002 to EC 2.3.3.11]
 
 
EC 2.3.3.12     
Accepted name: 3-propylmalate synthase
Reaction: pentanoyl-CoA + H2O + glyoxylate = 3-propylmalate + CoA
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]
[EC 2.3.3.12 created 1972 as EC 4.1.3.11, transferred 2002 to EC 2.3.3.12]
 
 
EC 2.3.3.13     
Accepted name: 2-isopropylmalate synthase
Reaction: acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA
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]
[EC 2.3.3.13 created 1972 as EC 4.1.3.12, transferred 2002 to EC 2.3.3.13]
 
 
EC 2.3.3.14     
Accepted name: homocitrate synthase
Reaction: acetyl-CoA + H2O + 2-oxoglutarate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
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, 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]
[EC 2.3.3.14 created 1972 as EC 4.1.3.21, transferred 2002 to EC 2.3.3.14]
 
 
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]
[EC 2.3.3.15 created 2003]
 
 
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
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]
[EC 2.3.3.16 created 2014]
 
 
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
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]
[EC 2.3.3.17 created 2016]
 
 
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]
[EC 2.3.3.18 created 2017]
 
 
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]
[EC 2.3.3.19 created 2017]
 
 


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