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Your query returned 6 entries. Printable version
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 | ||||||||||
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EC | 1.2.7.2 | ||||||||||
Deleted entry: | 2-oxobutyrate synthase. Now included with EC 1.2.7.1, pyruvate synthase. | ||||||||||
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 | ||||||||||
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EC | 2.3.1.182 | ||||||||||
Transferred entry: | (R)-citramalate synthase. Now classified as EC 2.3.3.21, (R)-citramalate synthase. | ||||||||||
EC | 2.3.3.21 | ||||||||||
Accepted name: | (R)-citramalate synthase | ||||||||||
Reaction: | acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate | ||||||||||
Glossary: | (2R)-2-hydroxy-2-methylbutanedioate = (2R)-2-methylmalate = (–)-citramalate 3-methyl-2-oxobutanoate = α-ketoisovalerate 2-oxobutanoate = α-ketobutyrate 4-methyl-2-oxopentanoate = α-ketoisocaproate 2-oxohexanoate = α-ketopimelate 2-oxoglutarate = α-ketoglutarate |
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Other name(s): | CimA | ||||||||||
Comments: | One of the enzymes involved in a pyruvate-derived pathway for isoleucine biosynthesis that is found in some bacterial and archaeal species [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 | ||||||||||
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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 | ||||||||||
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