| EC |
1.2.7.6 |
| Accepted name: |
glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) |
| Reaction: |
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin |
| Other name(s): |
GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase |
| Systematic name: |
D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase |
| Comments: |
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 162995-20-2 |
| References: |
| 1. |
Mukund, S. and Adams, M.W.W. 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 (1995) 8389–8392. [DOI] [PMID: 7721730] |
| 2. |
Roy, R., Menon, A.L. and Adams, M.W.W. Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331 (2001) 132–144. [DOI] [PMID: 11265456] |
|
| [EC 1.2.7.6 created 2003] |
| |
|
| |
|
Printable version