EC |
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+ |
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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, Gene, 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] |
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[EC 1.2.1.12 created 1961] |
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