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 / EGO
Search PMC articles PubMed articles NCBI proteins

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.

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): 8389–92. 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: 132–44. doi:10.1016/S0076-6879(01)31052-2. ISBN 978-0-12-182232-3. PMID 11265456.