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EC 1.2.7.7 Details
show Brenda entryEC number
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)
Comment
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.
History
created 2003
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.2.7.9 created 2003, deleted 2005 1.6.4.1 created 1961, deleted 2002 1.6.4.2 created 1961, modified 1989, deleted 2002 1.6.4.3 created 1961, modified 1976, deleted 1983 1.6.4.4 created 1965, deleted 2002 1.6.4.5 created 1972, deleted 2002 1.6.4.6 created 1972, deleted 2002 1.6.4.7 created 1978, deleted 2002 1.6.4.8 created 1989, deleted 2002 1.6.4.9 created 1992, deleted 2002 1.6.4.10 created 1992, deleted 2002
