Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.1.13 | ||||||||
| CAS number | 37250-87-6 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) (EC 1.2.1.13) is an enzyme that catalyzes the chemical reaction
- D-glyceraldehyde 3-phosphate + phosphate + NADP+ 3-phospho-D-glyceroyl phosphate + NADPH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NADP+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADPH, and H+.
Function
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. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway.
Nomenclature
The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating). Other names in common use include:
- dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
- GAPDH
- glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
- glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating)
- NADP-dependent glyceraldehyde phosphate dehydrogenase
- NADP-glyceraldehyde phosphate dehydrogenase
- NADP-glyceraldehyde-3-phosphate dehydrogenase
- NADP-triose phosphate dehydrogenase
- triosephosphate dehydrogenase (NADP)
References
Further reading
- Brenneman FN, Volk WA (1959). "Glyceraldehyde phosphate dehydrogenase activity with triphosphopyridine nucleotide and with diphosphopyridine nucleotide". J. Biol. Chem. 234: 2443–7. PMID 13804190.
- Gibbs M (1955). "TPN triosephosphate dehydrogenase from plant tissue". Methods Enzymol. 1: 411–415. doi:10.1016/0076-6879(55)01067-7.
- Rosenberg LL, Arnon DI (1955). "The preparation and properties of a new glyceraldehyde-3-phosphate dehydrogenase from photosynthetic tissues". J. Biol. Chem. 217 (1): 361–71. PMID 13271400.
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