Lactaldehyde reductase (NADPH) (EC 1.1.1.55) is an enzyme that catalyzes the chemical reaction:
propane-1,2-diol + NADP⁺ ⇌ (S)-lactaldehyde + NADPH + H⁺
The two substrates of this enzyme are propane-1,2-diol (propylene glycol) and NADP⁺ (oxidized nicotinamide adenine dinucleotide phosphate). Its three products are L-lactaldehyde, NADPH, and a proton.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is propane-1,2-diol:NADP⁺ oxidoreductase.
Other names in common use include:
- Lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase
- NADP⁺-1,2-propanediol dehydrogenase
- Propanediol dehydrogenase
- 1,2-Propanediol:NADP⁺ oxidoreductase
Classification identifiers:
- EC number: 1.1.1.55
- CAS number: 9028-43-7
The enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism. It was first characterized by Gupta and Robinson in 1960, who described the enzymatic conversion of lactaldehyde to propanediol (Journal of Biological Chemistry, 235(6): 1609–1612). The enzyme holds relevance in pharmaceutical and chemical industries due to its role in producing propane-1,2-diol and L-lactaldehyde, which serve as stereochemical building blocks for the synthesis of biologically active small molecules.
