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Glyceraldehyde-3-phosphate dehydrogenase (NADP+)

Enzyme

Enzyme

FieldValue
NameGlyceraldehyde-3-phosphate dehydrogenase (NADP+)
EC_number1.2.1.9
CAS_number9028-92-6
GO_code0008886

Glyceraldehyde-3-phosphate dehydrogenase (NADP+) () (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 the reaction:

Glyceraldehyde-3-phosphate dehydrogenase takes the same substrate but converts it to 1,3-bisphosphoglyceric acid, adding a phosphate group (Pi):

References

References

  1. (1955). "The preparation and properties of a new glyceraldehyde-3-phosphate dehydrogenase from photosynthetic tissues". J. Biol. Chem..
  2. (1995). "Sequence, expression, and function of the gene for the nonphosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans". J. Bacteriol..
  3. {{KEGG enzyme. 1.2.1.9
  4. {{KEGG enzyme. 1.2.1.12
Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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