3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)

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 dehydrogenase (ferredoxin)
Identifiers
EC no.1.2.7.7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin 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.

References

edit
  • 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 (3): 780–7. doi:10.1128/jb.178.3.780-787.1996. PMC 177725. 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 (3): 862–8. doi:10.1111/j.1432-1033.1997.00862.x. PMID 9108258.
  • Schut GJ, Menon AL, Adams MW (2001). "2-keto acid oxidoreductases from Pyrococcus furiosus and Thennococcus litoralis". 2-keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. Vol. 331. pp. 144–58. doi:10.1016/S0076-6879(01)31053-4. ISBN 978-0-12-182232-3. PMID 11265457.