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Lactaldehyde reductase

From Wikipedia, the free encyclopedia

In enzymology, a lactaldehyde reductase (EC 1.1.1.77) is an enzyme that catalyzes the chemical reaction

(R)[or (S)]-propane-1,2-diol + NAD+ (R)[or (S)]-lactaldehyde + NADH + H+

The 3 substrates of this enzyme are (R)-propane-1,2-diol, (S)-propane-1,2-diol, and NAD+, whereas its 4 products are (R)-lactaldehyde, (S)-lactaldehyde, 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)[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 1RRM, 2BI4, and 2BL4.

References

  • Ting SM, Sellinger OZ, Miller ON (1964). "The metabolism of lactaldehyde. VI. The reduction of D- and L-lactaldehyde in rat liver". Biochim. Biophys. Acta. 89: 217–225. doi:10.1016/0926-6569(64)90210-x. PMID 14203169.


This page was last edited on 26 August 2023, at 14:42
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