(R)-aminopropanol dehydrogenase
In enzymology, a (R)-aminopropanol dehydrogenase (EC 1.1.1.75) 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
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|