1.2.7.7: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
This is an abbreviated version!
For detailed information about 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin), go to the full flat file.
Word Map on EC 1.2.7.7
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1.2.7.7
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hyperthermophilic
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thermococcus
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archaeon
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pyrococcus
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indolepyruvate
-
furiosus
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thiamine
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ferredoxin-type
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co2
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paramagnetic
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a-dependent
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synthesis
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2-oxoglutarate
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pyrophosphate
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2-ketoacids
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beauveria
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beauvericin
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2-ketoglutarate
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bassiana
- 1.2.7.7
-
hyperthermophilic
- thermococcus
- archaeon
- pyrococcus
- indolepyruvate
- furiosus
- thiamine
-
ferredoxin-type
- co2
-
paramagnetic
-
a-dependent
- synthesis
- 2-oxoglutarate
- pyrophosphate
-
2-ketoacids
-
beauveria
- beauvericin
- 2-ketoglutarate
- bassiana
Reaction
+ + 2 oxidized ferredoxin = + + 2 reduced ferredoxin + 2 H+
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, VOR
ECTree
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Systematic Name
Systematic Name on EC 1.2.7.7 - 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
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3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
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.