(R)-aminopropanol dehydrogenase

Class of enzymes From Wikipedia, the free encyclopedia

In enzymology, a (R)-aminopropanol dehydrogenase (EC 1.1.1.75) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
 

The two substrates of this enzyme are (2R)-1-aminopropan-2-ol and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are aminoacetone, reduced NADH, and a proton.[1][2][3][4]

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.

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