D-malate dehydrogenase (decarboxylating)

D-malate dehydrogenase (decarboxylating)
Identifiers
EC no.1.1.1.83
CAS no.37250-20-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
 
H+
 
+ CO2 + NADH
 

The two substrates of this enzyme are D-malic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are pyruvic acid, carbon dioxide, reduced NADH, and a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). This enzyme participates in butanoate metabolism.

References

  1. ^ Enzyme 1.1.1.83 at KEGG Pathway Database.
  2. ^ Stern JR, O'Brien RW (1969). "Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes". J. Bacteriol. 98 (1): 147–51. doi:10.1128/JB.98.1.147-151.1969. PMC 249916. PMID 4889267.