EC 1.2.1.59 - Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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IntEnz Enzyme Nomenclature
EC 1.2.1.59

Names

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)

Reaction

Comments:

NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 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]

References

  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 1.2.1.59 created 1999]