Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
| glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) | |||||||||
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| Identifiers | |||||||||
| EC no. | 1.2.1.12 | ||||||||
| CAS no. | 9001-50-7 | ||||||||
| 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 | ||||||||
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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) is an enzyme that catalyzes the chemical reaction
- D-glyceraldehyde 3-phosphate + phosphate + NAD+ 3-phospho-D-glyceroyl phosphate + NADH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADH, and H+. This enzyme participates in glycolysis / gluconeogenesis.
Nomenclature
[edit]This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase.
References
[edit]Further reading
[edit]- Caputto R, Dixon M (1945). "Crystallization and identity of the triose and triosephosphate dehydrogenases of muscle". Nature. 156 (3969): 630–631. Bibcode:1945Natur.156..630.. doi:10.1038/156630c0. PMID 21006487. S2CID 4104880.
- Cori GT; Slein MW (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173 (2): 605–618. doi:10.1016/S0021-9258(18)57432-9. PMID 18910716.
- Hageman RH, Arnon DI (March 1955). "The isolation of triosephosphate dehydrogenase from pea seeds". Archives of Biochemistry and Biophysics. 55 (1): 162–8. doi:10.1016/0003-9861(55)90554-3. PMID 14362612.
- Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 243–273.
- Warburg O, Christian W (1939). "Isolierung und Krystallisation des Proteins des oxydierenden Garungsferments". Biochem. Z. 303: 40–68.
