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+
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. PMID 4310089.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|