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Words near each other
・ Glyceollin
・ Glyceollin I
・ Glyceollin III
・ Glyceollin synthase
・ Glycera
・ Glycera (courtesan)
・ Glycera (genus)
・ Glyceraldehyde
・ Glyceraldehyde 3-phosphate
・ Glyceraldehyde 3-phosphate dehydrogenase
・ Glyceraldehyde-3-phosphate dehydrogenase (disambiguation)
・ Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
・ Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)
・ Glyceraldehyde-3-phosphate dehydrogenase (NADP+)
・ Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)
Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
・ Glycerate 2-kinase
・ Glycerate dehydrogenase
・ Glycerate kinase
・ Glyceria
・ Glyceria borealis
・ Glyceria fluitans
・ Glyceria grandis
・ Glyceria leptostachya
・ Glyceria maxima
・ Glyceria notata
・ Glyceria striata
・ Glyceric acid
・ Glyceridae
・ Glyceride


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Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) : ウィキペディア英語版
Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) () is an enzyme that catalyzes the chemical reaction
:D-glyceraldehyde 3-phosphate + phosphate + NAD+ \rightleftharpoons 3-phospho-D-glyceroyl phosphate + NADH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase. This enzyme participates in glycolysis / gluconeogenesis.
==Structural studies==

As of late 2007, 49 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .

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