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(R)-aminopropanol dehydrogenase : ウィキペディア英語版 | (R)-aminopropanol dehydrogenase
In enzymology, a (R)-aminopropanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(R)-1-aminopropan-2-ol + NAD+ aminoacetone + NADH + H+ Thus, the two substrates of this enzyme are (R)-1-aminopropan-2-ol and NAD+, whereas its 3 products are aminoacetone, NADH, 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 (R)-1-aminopropan-2-ol:NAD+ oxidoreductase. Other names in common use include L-aminopropanol dehydrogenase, 1-aminopropan-2-ol-NAD+ dehydrogenase, L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase, 1-aminopropan-2-ol-dehydrogenase, DL-1-aminopropan-2-ol: NAD+ dehydrogenase, and L(+)-1-aminopropan-2-ol-NAD+/NADP+ oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It requires potassium as a cofactor. ==References==
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