Indolepyruvate ferredoxin oxidoreductase

In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction

indolepyruvate ferredoxin oxidoreductase
Identifiers
EC no.1.2.7.8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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Gene OntologyAmiGO / QuickGO
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NCBIproteins
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin

The 3 substrates of this enzyme are (indol-3-yl)pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are S-2-(indol-3-yl)acetyl-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 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating). Other names in common use include 3-(indol-3-yl)pyruvate synthase (ferredoxin), and IOR.

References

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  • Mai X, Adams MW (1994). "Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A new enzyme involved in peptide fermentation". J. Biol. Chem. 269 (24): 16726–32. doi:10.1016/S0021-9258(19)89451-6. PMID 8206994.
  • Siddiqui MA, Fujiwara S, Imanaka T (1997). "Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1 possesses a mosaic structure showing features of various oxidoreductases". Mol. Gen. Genet. 254 (4): 433–9. doi:10.1007/PL00008607. PMID 9180697.
  • 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.