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3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
Identifiers
EC no. 1.2.7.7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

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 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

  • 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.