ExplorEnz: EC 1.2.1.90

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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 (ambiguous); 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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15288789]

[EC 1.2.1.90 created 2014]