Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
|glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)|
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
- 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.
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.
- Caputto R, Dixon M (1945). "Crystallization and identity of the triose and triosephosphate dehydrogenases of muscle". Nature. 156: 630. PMID 21006487.
- Cori GT; Slein MW (1948). "Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle". J. Biol. Chem. 173: 605–618.
- 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. 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.
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