Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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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

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+ \rightleftharpoons 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[edit]

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[edit]

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[edit]

Further reading[edit]

  • 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.