Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)

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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction

D-glyceraldehyde-3-phosphate + H₂O + 2 oxidized ferredoxin $\rightleftharpoons$ 3-phospho-D-glycerate + 2 H⁺ + 2 reduced ferredoxin

The 3 substrates of this enzyme are D-glyceraldehyde-3-phosphate, H₂O, and oxidized ferredoxin, whereas its 3 products are 3-phospho-D-glycerate, 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 D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase.

[edit] References

IUBMB entry for 1.2.7.6
BRENDA references for 1.2.7.6 (Recommended.)
PubMed references for 1.2.7.6
PubMed Central references for 1.2.7.6
Google Scholar references for 1.2.7.6
Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus". J. Biol. Chem. 270: 8389–92. doi:10.1074/jbc.270.15.8389. PMID 7721730.
Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods. Enzymol. 331: 132–44. PMID 11265456.