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Glyceraldehyde-3-phosphate dehydrogenase (NADP+)

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Enzyme
Glyceraldehyde-3-phosphate dehydrogenase (NADP+)
Identifiers
EC no.1.2.1.9
CAS no.9028-92-6
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Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (EC 1.2.1.9) (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. It has been found in plants, algae, and bacteria.

Reactions

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 / >> 1 >> / .

See also

References

  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.
Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP
1.2.2: cytochrome
1.2.3: oxygen
1.2.4: disulfide
1.2.7: iron–sulfur protein
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