IUBMB Enzyme Nomenclature

EC 1.2.1.90

Accepted name: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]

Reaction: D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+

Other name(s): non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; GAPN

Systematic name: D-glyceraldehyde-3-phosphate:NAD(P)+ oxidoreductase

Comments: The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Brunner, N.A., Brinkmann, H., Siebers, B. and Hensel, R. NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J. Biol. Chem. 273 (1998) 6149-6156. [PMID: 9497334]

2. Brunner, N.A., Siebers, B. and Hensel, R. Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level. Extremophiles 5 (2001) 101-109. [PMID: 11354453]

3. Pohl, E., Brunner, N., Wilmanns, M. and Hensel, R. The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax. J. Biol. Chem. 277 (2002) 19938-19945. [PMID: 11842090]

4. Lorentzen, E., Hensel, R., Knura, T., Ahmed, H. and Pohl, E. Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax. J. Mol. Biol. 341 (2004) 815-828. [PMID: 15288789]

[EC 1.2.1.90 created 2014]


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