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 | ||||||
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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
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). [11] Aldehyde Oxidoreductases from Pyrococcus furiosus. "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol.. Methods in Enzymology 331: 132–44. doi:10.1016/S0076-6879(01)31052-2. ISBN 9780121822323. PMID 11265456.