Lactaldehyde dehydrogenase

Last updated
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
Search
PMC articles
PubMed articles
NCBI proteins

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

+ NAD+
 
 
H2O
H+
Lactaldehyde dehydrogenase
H2O
H+
 
+ NADH
 

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

  1. Enzyme 1.2.1.22 at KEGG Pathway Database.
  2. 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.
  3. 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.