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Aspartate dehydrogenase : ウィキペディア英語版 | Aspartate dehydrogenase
Aspartate dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-aspartate + H2O + NAD(P)+ oxaloacetate + NH3 + NAD(P)H + H+ The 4 substrates of this enzyme are L-aspartate, water, nicotinamide adenine dinucleotide ion, and nicotinamide adenine dinucleotide phosphate ion, whereas its 5 products are oxaloacetate, ammonia, NADH, nicotinamide adenine dinucleotide phosphate, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD-dependent aspartate dehydrogenase, NADH2-dependent aspartate dehydrogenase, and NADP+-dependent aspartate dehydrogenase. This enzyme participates in nicotinate and nicotinamide 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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