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 (R)-propane-1,2-diol it produces (R)-lactaldehyde but the enantiomeric substrate (S)-propane-1,2-diol gives only (S)-lactaldehyde. The enzyme's cofactor is nicotinamide adenine dinucleotide (NAD⁺), 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 (R)[or (S)]-propane-1,2-diol:NAD⁺ oxidoreductase. Other names in common use include propanediol:nicotinamide adenine dinucleotide (NAD⁺) 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 .

References