3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)

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In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) (EC 1.2.7.7) is an enzyme that catalyzes the chemical reaction

3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin $\rightleftharpoons$ S-(2-methylpropanoyl)-CoA + CO₂ + reduced ferredoxin

The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 products are S-(2-methylpropanoyl)-CoA, CO₂, and reduced ferredoxin.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is '. Other names in common use include 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, and 2-oxoisovalerate ferredoxin reductase.

[edit] References

IUBMB entry for 1.2.7.7
BRENDA references for 1.2.7.7 (Recommended.)
PubMed references for 1.2.7.7
PubMed Central references for 1.2.7.7
Google Scholar references for 1.2.7.7
Heider J, Mai X, Adams MW (1996). "Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea". J. Bacteriol. 178: 780–7. PMID 8550513.
Tersteegen A, Linder D, Thauer RK, Hedderich R (1997). "Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum". Eur. J. Biochem. 244: 862–8. PMID 9108258.
Schut GJ, Menon AL, Adams MW (2001). "2-keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis". Methods. Enzymol. 331: 144–58. PMID 11265457.