Enzyme Nomenclature

EC 2.3.3

Acyl groups converted into alkyl on transfer

Continued from EC 2.3.2

Contents

EC 2.3.3.1 citrate (Si)-synthase
EC 2.3.3.2 decylcitrate synthase
EC 2.3.3.3 citrate (Re)-synthase
EC 2.3.3.4 decylhomocitrate synthase
EC 2.3.3.5 2-methylcitrate synthase
EC 2.3.3.6 2-ethylmalate synthase
EC 2.3.3.7 3-ethylmalate synthase
EC 2.3.3.8 ATP citrate synthase
EC 2.3.3.9 malate synthase
EC 2.3.3.10 hydroxymethylglutaryl-CoA synthase
EC 2.3.3.11 2-hydroxyglutarate synthase
EC 2.3.3.12 3-propylmalate synthase
EC 2.3.3.13 2-isopropylmalate synthase
EC 2.3.3.14 homocitrate synthase
EC 2.3.3.15 sulfoacetaldehyde acetyltransferase EC 2.3.3.16 citrate synthase (unknown stereospecificity)
EC 2.3.3.17 methylthioalkylmalate synthase
EC 2.3.3.18 2-phosphinomethylmalate synthase
EC 2.3.3.19 2-phosphonomethylmalate synthase
EC 2.3.3.20 acyl-CoA:acyl-CoA alkyltransferase


Entries

EC 2.3.3.1

Accepted name: citrate (Si)-synthase

Reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA

For diagram of reaction click here or 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 C2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase.

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. [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 2.3.3.2

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]

[EC 2.3.3.2 created 1972 as EC 4.1.3.23, transferred 2002 to EC 2.3.3.2]

EC 2.3.3.3

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]

[EC 2.3.3.3 created 1972 as EC 4.1.3.28, transferred 2002 to EC 2.3.3.3]

EC 2.3.3.4

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.

[EC 2.3.3.4 created 1976 as EC 4.1.3.29, transferred 2002 to EC 2.3.3.4]

EC 2.3.3.5

Accepted name: 2-methylcitrate synthase

Reaction: propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA

For diagram of reaction click here.

Glossary: 2-methylcitrate = (2S,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 is distinct 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, 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. Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184-6194. [PMID: 12473114]

5. Domin, N., Wilson, D. and Brock, M. Methylcitrate cycle activation during adaptation of Fusarium solani and Fusarium verticillioides to propionyl-CoA-generating carbon sources. Microbiology 155 (2009) 3903-3912. [PMID: 19661181]

[EC 2.3.3.5 created 1978 as EC 4.1.3.31, transferred 2002 to EC 2.3.3.5, modified 2015]

EC 2.3.3.6

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]

[EC 2.3.3.6 created 1983 as EC 4.1.3.33, transferred 2002 to EC 2.3.3.6]

EC 2.3.3.7

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.

[EC 2.3.3.7 created 1965 as EC 4.1.3.10, modified 1983, transferred 2002 to EC 2.3.3.10]

EC 2.3.3.8

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.

[EC 2.3.3.8 created 1965 as EC 4.1.3.8, modified 1986, transferred 2002 to EC 2.3.3.8]

EC 2.3.3.9

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; acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)

Systematic name: acetyl-CoA:glyoxylate C-acetyltransferase [(S)-malate-forming]

Comments: The enzyme catalyses the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2.

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]

[EC 2.3.3.9 created 1961 as EC 4.1.3.2, transferred 2002 to EC 2.3.3.9]

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 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.

[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.

[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 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.

[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 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]

[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 = (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]

[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. [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 C2 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, CAS registry number:

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. [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. [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 reaction 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, CAS registry number:

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. [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. [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, CAS registry number:

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, CAS registry number:

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. [PMID: 18721747]

[EC 2.3.3.19 created 2017]

EC 2.3.3.20

Accepted name: acyl-CoA:acyl-CoA alkyltransferase

Reaction: 2 an acyl-CoA + H2O = a (2R)-2-alkyl-3-oxoalkanoate + 2 CoA

Other name(s): oleA (gene name)

Systematic name: acyl-CoA:acyl-CoA alkyltransferase [(2R)-2-alkyl-3-oxoalkanoate-forming]

Comments: The enzyme, found in certain bacterial species, catalyses a head-to-head non-decarboxylative Claisen condensation of two acyl-CoA molecules, resulting in formation of a 2-alkyl-3-oxoalkanoic acid. It is part of a pathway for the production of olefins.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sukovich, D.J., Seffernick, J.L., Richman, J.E., Hunt, K.A., Gralnick, J.A. and Wackett, L.P. Structure, function, and insights into the biosynthesis of a head-to-head hydrocarbon in Shewanella oneidensis strain MR-1. Appl. Environ. Microbiol. 76 (2010) 3842-3849. [PMID: 20418444]

2. Frias, J.A., Richman, J.E., Erickson, J.S. and Wackett, L.P. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J. Biol. Chem. 286 (2011) 10930-10938. [PMID: 21266575]

3. Goblirsch, B.R., Frias, J.A., Wackett, L.P. and Wilmot, C.M. Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids. Biochemistry 51 (2012) 4138-4146. [PMID: 22524624]

4. Goblirsch, B.R., Jensen, M.R., Mohamed, F.A., Wackett, L.P. and Wilmot, C.M. Substrate trapping in crystals of the thiolase OleA identifies three channels that enable long chain olefin biosynthesis. J. Biol. Chem. 291 (2016) 26698-26706. [PMID: 27815501]

[EC 2.3.3.20 created 2018]


Continued with EC 2.4.1.1 to EC 2.4.1.50
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