D-malate dehydrogenase (decarboxylating)
Appearance
D-malate dehydrogenase (decarboxylating) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.83 | ||||||||
CAS no. | 37250-20-7 | ||||||||
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 | ||||||||
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In enzymology, a D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) is an enzyme that catalyzes the chemical reaction
- (R)-malate + NAD+ pyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH.
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
[edit]- 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.