Glyceraldehyde-3-phosphate dehydrogenase (NADP+)

Enzyme From Wikipedia, the free encyclopedia

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.[1] It has been found in plants, algae, and bacteria.[2]

Reactions

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

 
 
H2O
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
H2O
H+
 
 

Glyceraldehyde-3-phosphate dehydrogenase takes the same substrate but converts it to 1,3-bisphosphoglyceric acid, adding a phosphate group (Pi):[4]

2D representation of the chemical structure of Q26992303.
D-glyceraldehyde 3-phosphate
+ NAD+
 
 
Pi
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
Pi
H+
 
 

See also

References

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