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Information on EC 1.2.7.7 - 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)

for references in articles please use BRENDA:EC1.2.7.7
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IUBMB 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.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-ketoisovalerate ferredoxin oxidoreductase, 2-oxoisovalerate ferredoxin reductase, 2-oxoisovalerate oxidoreductase, 2-oxoisovalerate:ferredoxin oxidoreductase, 3-methyl-2-oxobutanoate dehydrogenase, 3-methyl-2-oxobutanoate synthase (ferredoxin), branched-chain ketoacid ferredoxin reductase, branched-chain oxo acid ferredoxin reductase, keto-valine-ferredoxin oxidoreductase, ketoisovalerate ferredoxin reductase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+
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