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In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction

(S)-lactaldehyde + NAD + H₂O ${\displaystyle \rightleftharpoons }$ (S)-lactate + NADH + 2 H

The 3 substrates of this enzyme are (S)-lactaldehyde, NAD, and H₂O, whereas its 3 products are (S)-lactate, NADH, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2HG2, 2ILU, 2IMP, and 2OPX.

References

• Rembold H, Simmersbach F (1969). "Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver". Biochim. Biophys. Acta. 184 (3): 589–96. doi:10.1016/0304-4165(69)90273-6. PMID 5821022.
• Sridhara S, Wu TT (1969). "Purification and properties of lactaldehyde dehydrogenase from Escherichia coli". J. Biol. Chem. 244 (19): 5233–8. doi:10.1016/S0021-9258(18)63651-8. PMID 4310089.

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