Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
For reaction pathway click here.
Other name(s): triosephosphate dehydrogenase (ambiguous); 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; glyceraldehyde-3-P-dehydrogenase
Systematic name: D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Comments: Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-50-7
References:
1. Caputto, R. and Dixon, M. Crystallization and identity of the triose and triosephosphate dehydrogenase of muscle. Nature (Lond.) 156 (1945) 630-631.
2. Cori, G.T., Slein, M.W. and Cori, C.F. Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. J. Biol. Chem. 173 (1948) 605-618.
3. Hageman, R.H. and Arnon, D.I. The isolation of triosephosphate dehydrogenase from pea seeds. Arch. Biochem. Biophys. 55 (1955) 162-168.
4. Velick, S.F. and Furfine, C. Glyceraldehyde 3-phosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 243-273.
5. Warburg, O. and Christian, W. Isolierung und Krystallisation des Proteins des oxydierenden Gärungsferments. Biochem. Z. 303 (1939) 40-68.
6. Ryzlak, M.T. and Pietruszko, R. Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain. Biochim. Biophys. Acta 954 (1988) 309–324. [PMID: 3370218]