ExplorEnz: EC 1.2.1.12

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1.2.1.12

Accepted name:

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

Reaction:

D-glyceraldehyde 3-phosphate + phosphate + NAD⁺ = 3-phospho-D-glyceroyl phosphate + NADH + H⁺

For diagram of reaction, click here

Other name(s):

triosephosphate dehydrogenase (ambiguous); glyceraldehyde phosphate dehydrogenase; 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. [PMID: 18910716]
3.	Hageman, R.H. and Arnon, D.I. The isolation of triosephosphate dehydrogenase from pea seeds. Arch. Biochem. Biophys. 55 (1955) 162–168. [DOI] [PMID: 14362612]
4.	Velick, S.F. and Furfine, C. Glyceraldehyde 3-phosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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. [DOI] [PMID: 3370218]

[EC 1.2.1.12 created 1961]