Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)

glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
Identifiers
EC number 1.2.7.6
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

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 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.

References

    • 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 (15): 8389&ndash, 92. doi:10.1074/jbc.270.15.8389. PMID 7721730.
    • Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. 331: 132&ndash, 44. doi:10.1016/S0076-6879(01)31052-2. ISBN 978-0-12-182232-3. PMID 11265456.


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