Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)
| glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.59 | ||||||||
| CAS no. | 39369-25-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (EC 1.2.1.59) is an enzyme that catalyzes the chemical reaction
- D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
The 4 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, NAD+, and NADP+, whereas its 4 products are 3-phospho-D-glyceroyl phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating). Other names in common use include (phosphorylating), triosephosphate dehydrogenase (NAD(P)), and glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CZC.
References
- P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962.
- Valverde F, Losada M, Serrano A (1997). "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 (14): 4513–22. doi:10.1128/jb.179.14.4513-4522.1997. PMC 179286. PMID 9226260.
