D-lactate dehydrogenase (cytochrome)

In enzymology, a D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction

(D)-lactate + 2 ferricytochrome c pyruvate + 2 ferrocytochrome c
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

Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.

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 employs one cofactor, FAD. This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants . It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.