Lactaldehyde dehydrogenase

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

(S)-lactaldehyde + NAD+ + H2O (S)-lactate + NADH + 2 H+
lactaldehyde dehydrogenase
Identifiers
EC number1.2.1.22
CAS number37250-90-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

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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. PMID 4310089.


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