D-lactate dehydrogenase (cytochrome)

D-lactate dehydrogenase (cytochrome)
Identifiers
EC no.1.1.2.4
CAS no.37250-79-6
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, D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction

 
Fe3+
Fe2+
Fe3+
Fe2+
 
+ 2 H+
 

The substrate of this enzyme is (R)-lactic acid, which is acted on by two equivalents of the cofactor, ferricytochrome c, which oxidises the hydroxy group to a keto group, giving pyruvic acid, while the cofactor's iron is reduced.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (D)-lactate:ferricytochrome-c 2-oxidoreductase. Other names in common use include lactic acid dehydrogenase, D-lactate (cytochrome) dehydrogenase, cytochrome-dependent D-(−)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(−)-lactic cytochrome c reductase. This enzyme participates in pyruvate metabolism. It is a flavoprotein. This type of enzyme has been characterized in animals, fungi, bacteria and plants. It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway.