The Enzyme Database

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EC 1.2.7.1     
Accepted name: pyruvate synthase
Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase; 2-oxobutyrate synthase; α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase; 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating); 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9082-51-3
References:
1.  Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420–1425. [DOI] [PMID: 5217644]
2.  Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963–6969. [PMID: 4628267]
3.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111–3119. [PMID: 5574389]
4.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120–3125. [PMID: 4324891]
5.  Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663–669. [DOI] [PMID: 10607667]
[EC 1.2.7.1 created 1972, modified 2003, modified 2013]
 
 
EC 1.2.7.2      
Deleted entry: 2-oxobutyrate synthase. Now included with EC 1.2.7.1, pyruvate synthase.
[EC 1.2.7.2 created 1972, deleted 2013]
 
 
EC 1.2.7.7     
Accepted name: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
Reaction: 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase
Systematic name: 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
Comments: The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, and 2-oxobutanoate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyse the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Buchanan, B.B. Role of ferredoxin in the synthesis of α-ketobutyrate from propionyl coenzyme A and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria. J. Biol. Chem. 244 (1969) 4218–4223. [PMID: 5800441]
2.  Heider, J., Mai, X.H. and Adams, M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 178 (1996) 780–787. [DOI] [PMID: 8550513]
3.  Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862–868. [DOI] [PMID: 9108258]
4.  Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144–158. [DOI] [PMID: 11265457]
[EC 1.2.7.7 created 2003]
 
 
EC 2.3.1.182     
Accepted name: (R)-citramalate synthase
Reaction: acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate
Glossary: (-)-citramalate = (2R)-2-methylmalate = (2R)-2-hydroxy-2-methylbutanedioate
α-ketoisovalerate = 3-methyl-2-oxobutanoate
α-ketobutyrate = 2-oxobutanoate
α-ketoisocaproate = 4-methyl-2-oxopentanoate
α-ketopimelate = 2-oxohexanoate
α-ketoglutarate = 2-oxoglutarate
Other name(s): CimA
Comments: One of the enzymes involved in a novel pyruvate pathway for isoleucine biosynthesis that is found in some, mainly archaeal, bacteria [1,2]. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine [2]. The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Howell, D.M., Xu, H. and White, R.H. (R)-Citramalate synthase in methanogenic archaea. J. Bacteriol. 181 (1999) 331–333. [PMID: 9864346]
2.  Xu, H., Zhang, Y., Guo, X., Ren, S., Staempfli, A.A., Chiao, J., Jiang, W. and Zhao, G. Isoleucine biosynthesis in Leptospira interrogans serotype 1ai strain 56601 proceeds via a threonine-independent pathway. J. Bacteriol. 186 (2004) 5400–5409. [DOI] [PMID: 15292141]
[EC 2.3.1.182 created 2007]
 
 
EC 4.1.1.64     
Accepted name: 2,2-dialkylglycine decarboxylase (pyruvate)
Reaction: 2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
Other name(s): dialkyl amino acid (pyruvate) decarboxylase; α-dialkyl amino acid transaminase; 2,2-dialkyl-2-amino acid-pyruvate aminotransferase; L-alanine-α-ketobutyrate aminotransferase; dialkylamino-acid decarboxylase (pyruvate); 2,2-dialkylglycine carboxy-lyase (amino-transferring)
Systematic name: 2,2-dialkylglycine carboxy-lyase (amino-transferring; L-alanine-forming)
Comments: A pyridoxal-phosphate protein. Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-17-1
References:
1.  Bailey, G.B. and Dempsey, W.B. Purification and properties of an α-dialkyl amino acid transaminase. Biochemistry 6 (1967) 1526–1533.
[EC 4.1.1.64 created 1972]
 
 


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