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⁺ ${\displaystyle \rightleftharpoons }$ 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

• Dekker EE, Swain RR (1968). "Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli" (PDF). Biochim. Biophys. Acta. 158 (2): 306–7. doi:10.1016/0304-4165(68)90150-5. hdl:2027.42/33173. PMID 4385233.
• Tuner JM (1966). "Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli". Biochem. J. 99 (2): 427–33. PMC 1265012. PMID 5329339.
• Turner JM (1967). "Microbial metabolism of amino ketones: l-1-Aminopropan-2-ol dehydrogenase and l-threonine dehydrogenase in Escherichia coli". Biochem. J. 104 (1): 112–21. PMC 1270551. PMID 5340733.