In enzymology, D-lactate dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
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-(âÂÂ)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(âÂÂ)-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.