Methylglyoxal reductase (NADH-dependent)

methylglyoxal reductase (NADH-dependent)
Identifiers
EC no.1.1.1.78
CAS no.37250-16-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, methylglyoxal reductase (NADH-dependent) (EC 1.1.1.78) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
 
H+
 
 

The two substrates of this enzyme are (R)-lactaldehyde and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are methylglyoxal, reduced NADH, and a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include methylglyoxal reductase, and D-lactaldehyde dehydrogenase. This enzyme participates in pyruvate metabolism.

References

  1. ^ Enzyme 1.1.1.78 at KEGG Pathway Database.
  2. ^ Ting SM, Miller ON, Sellinger OZ (1965). "The Metabolism of lactaldehyde: VII. The oxidation of d-lactaldehyde in rat liver". Biochim. Biophys. Acta. 97: 407–15. doi:10.1016/0304-4165(65)90151-0. PMID 14323585.