Glyceraldehyde-3-phosphate dehydrogenase (NADP+)

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Glyceraldehyde-3-phosphate dehydrogenase (NADP+)
EC no.
CAS no.9028-92-6
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (EC (GAPN) is an enzyme that irreversibly catalyzes the oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3-PG or 3-PGA) using the reduction of NADP+ to NADPH. GAPN is used in a variant of glycolysis that conserves energy as NADPH rather than as ATP. The NADPH and 3-PG can then be used for synthesis. The most familiar variant of glycolysis uses glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase to produce ATP. GAPDH is phosphorylating. GAPN is non-phosphorylating.

GAPN was reported first by Rosenberg and Arnon in 1954.[1] It has been found in plants, algae, and bacteria.[2]


Glyceraldehyde-3-phosphate dehydrogenase (NADP+) catalyzes

GAP + NADP+ + H2O → 3-PG + NADPH + H+

Glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase catalyze

GAP + NAD+ + Pi ⇌ 1,3-bisphosphoglycerate + NADH + H+
1,3-bisphosphoglycerate + ADP ⇌ 3-PG + ATP

Usually [NADPH] / [NADP+] >> 1 >> [NADH] / [NAD+].

See also[edit]


  1. ^ 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.
  2. ^ Boyd DA, Cvitkovitch DG, Hamilton IR (1995). "Sequence, expression, and function of the gene for the nonphosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans". J. Bacteriol. 177 (10): 2622–7. PMC 176930. PMID 7751269.