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・ Glycerol dehydrogenase (acceptor)
・ Glycerol dehydrogenase (NADP+)
・ Glycerol ester of wood rosin
・ Glycerol kinase
・ Glycerol kinase deficiency
・ Glycerol monostearate
・ Glycerol phenylbutyrate
・ Glycerol phosphate shuttle
・ Glycerol-1,2-cyclic-phosphate 2-phosphodiesterase
・ Glycerol-1-phosphatase
・ Glycerol-2-phosphatase
・ Glycerol-3-phosphate 1-dehydrogenase (NADP+)
・ Glycerol-3-phosphate 2-O-acyltransferase
・ Glycerol-3-phosphate cytidylyltransferase
・ Glycerol-3-phosphate dehydrogenase
Glycerol-3-phosphate dehydrogenase (NAD(P)+)
・ Glycerol-3-phosphate dehydrogenase (NAD+)
・ Glycerol-3-phosphate dehydrogenase (quinone)
・ Glycerol-3-phosphate O-acyltransferase
・ Glycerol-3-phosphate oxidase
・ Glycerol-3-phosphate-transporting ATPase
・ Glycerol-3-phosphate—glucose phosphotransferase
・ Glycerolysis
・ Glycerone kinase
・ Glyceroneogenesis
・ Glyceronephosphate O-acyltransferase
・ Glycerophosphocholine cholinephosphodiesterase
・ Glycerophosphocholine phosphodiesterase
・ Glycerophosphodiester phosphodiesterase
・ Glycerophosphoinositol glycerophosphodiesterase


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Glycerol-3-phosphate dehydrogenase (NAD(P)+) : ウィキペディア英語版
Glycerol-3-phosphate dehydrogenase (NAD(P)+)

In enzymology, a glycerol-3-phosphate dehydrogenase () () is an enzyme that catalyzes the chemical reaction
:''sn''-glycerol 3-phosphate + NAD(P)+ \rightleftharpoons glycerone phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are sn-glycerol 3-phosphate, NAD+, and NADP+, whereas its 4 products are glycerone phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ''sn''-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase. Other names in common use include L-glycerol-3-phosphate:NAD(P)+ oxidoreductase, glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide, (phosphate)), glycerol 3-phosphate dehydrogenase (NADP+), and glycerol-3-phosphate dehydrogenase (). This enzyme participates in glycerophospholipid metabolism.
==Structural studies==

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .

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