Aldehyde ferredoxin oxidoreductase

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In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction

an aldehyde + H₂O + 2 oxidized ferredoxin $\rightleftharpoons$ an acid + 2 H⁺ + 2 reduced ferredoxin

The 3 substrates of this enzyme are aldehyde, H₂O, and oxidized ferredoxin, whereas its 3 products are acid, H⁺, 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 aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR.

[edit] References

IUBMB entry for 1.2.7.5
BRENDA references for 1.2.7.5 (Recommended.)
PubMed references for 1.2.7.5
PubMed Central references for 1.2.7.5
Google Scholar references for 1.2.7.5
Mukund S, Adams MW (1991). "The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway". J. Biol. Chem. 266: 14208–16. PMID 1907273.
Johnson JL, Rajagopalan KV, Mukund S, Adams MW (1993). "Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea". J. Biol. Chem. 268: 4848–52. PMID 8444863.
Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC (1995). "Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase". Science. 267: 1463–9. doi:10.1126/science.7878465. PMID 7878465.
Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods. Enzymol. 331: 132–44. PMID 11265456.