Reaction: a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Other name(s): OFOR
Systematic name: 2-oxocarboxylate:ferredoxin 2-oxidoreductase (decarboxylating, CoA-acylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters [2]. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For example, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kerscher, L. and Oesterhelt, D. Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium. Eur. J. Biochem. 116 (1981) 587-594. [PMID: 6266826]
2. Zhang, Q., Iwasaki, T., Wakagi, T. and Oshima, T. 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biochem. 120 (1996) 587-599. [PMID: 8902625]
3. Fukuda, E., Kino, H., Matsuzawa, H. and Wakagi, T. Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes. Eur. J. Biochem. 268 (2001) 5639-5646. [PMID: 11683888]
4. Fukuda, E. and Wakagi, T. Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7. Biochim. Biophys. Acta 1597 (2002) 74-80. [PMID: 12009405]
5. Nishizawa, Y., Yabuki, T., Fukuda, E. and Wakagi, T. Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1. FEBS Lett 579 (2005) 2319-2322. [PMID: 15848165]
6. Park, Y.J., Yoo, C.B., Choi, S.Y. and Lee, H.B. Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1. J. Biochem. Mol. Biol. 39 (2006) 46-54. [PMID: 16466637]