| 词条 | Glyceraldehyde-3-phosphate dehydrogenase (NADP+) |
| 释义 |
| Name = Glyceraldehyde-3-phosphate dehydrogenase (NADP+) | EC_number = 1.2.1.9 | CAS_number = 9028-92-6 | IUBMB_EC_number = 1/2/1/9 | GO_code = 0008886 | image = | width = | caption = }} Glyceraldehyde-3-phosphate dehydrogenase (NADP+) ({{EC number|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.[2] ReactionsGlyceraldehyde-3-phosphate dehydrogenase (NADP+) catalyzes GAP + NADP+ + H2O → 3-PG + NADPH + H+ Glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase catalyze GAP + NAD+ + Pi {{eqm}} 1,3-bisphosphoglycerate + NADH + H+ 1,3-bisphosphoglycerate + ADP {{eqm}} 3-PG + ATP Usually [NADPH] / [NADP+] >> 1 >> [NADH] / [NAD+]. See also
References1. ^1 {{cite journal |vauthors=Boyd DA, Cvitkovitch DG, Hamilton IR |year=1995 |title=Sequence, expression, and function of the gene for the nonphosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans |journal=J. Bacteriol. |volume=177 |issue=10 |pages=2622–7 |doi= |pmid=7751269 |pmc=176930}} [1]}}{{Aldehyde/Oxo oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}} 1 : EC 1.2.1 |
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