Lactaldehyde dehydrogenase
| lactaldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.22 | ||||||||
| CAS no. | 37250-90-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are (S)-lactaldehyde, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are (S)-lactic acid, reduced NADH, and a proton.[1][2][3]
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
- ^ Enzyme 1.2.1.22 at KEGG Pathway Database.
- ^ 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.