| glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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): 8389–92. doi: 10.1074/jbc.270.15.8389. PMID 7721730.
- Roy R, Menon AL, Adams MW (2001). "Aldehyde Oxidoreductases from Pyrococcus furiosus". Hyperthermophilic enzymes Part B. Methods in Enzymology. Vol. 331. pp. 132–44. doi: 10.1016/S0076-6879(01)31052-2. ISBN 978-0-12-182232-3. PMID 11265456.
| glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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): 8389–92. doi: 10.1074/jbc.270.15.8389. PMID 7721730.
- Roy R, Menon AL, Adams MW (2001). "Aldehyde Oxidoreductases from Pyrococcus furiosus". Hyperthermophilic enzymes Part B. Methods in Enzymology. Vol. 331. pp. 132–44. doi: 10.1016/S0076-6879(01)31052-2. ISBN 978-0-12-182232-3. PMID 11265456.