EC - Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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IntEnz Enzyme Nomenclature


Accepted name:
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
Other names:
triosephosphate dehydrogenase (NAD(P))
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
triosephosphate dehydrogenase (NAD(P)+)
Systematic name:
D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)



NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00069
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043891
CAS Registry Number: 39369-25-0
UniProtKB/Swiss-Prot: (61) [show] [UniProt]


  1. Valverde, F., Losada, M. and Serrano, A.
    Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase.
    In: P. Mathis (Ed.) Photosynthesis: From Light to Biosphere vol. 1 , Kluwer Academic Publishers , 1995 , 959-962
  2. Valverde, F., Losada, M. and Serrano, A.
    Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803.
    J. Bacteriol. 179 : 4513-4522 (1997). [PMID: 9226260]

[EC created 1999]