Lactaldehyde reductase


In enzymology, lactaldehyde reductase is an enzyme that catalyzes two chemical reactions
Each individual reaction is stereospecific so that when the substrate of the enzyme is -propane-1,2-diol it produces -lactaldehyde but the enantiomeric substrate -propane-1,2-diol gives only -lactaldehyde. The enzyme's cofactor is nicotinamide adenine dinucleotide, which is converted to NADH, and also releases a proton.
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 -propane-1,2-diol:NAD+ oxidoreductase. Other names in common use include propanediol:nicotinamide adenine dinucleotide oxidoreductase, and L-lactaldehyde:propanediol oxidoreductase. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes,, and.