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

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

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[1] .[2] It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway

References[]

  1. ^ Atlante, A.; de Bari, L.; Valenti, D.; Pizzuto, R.; Paventi, G. & Passarella, S. (2005). "Transport and metabolism of D-lactate in Jerusalem artichoke mitochondria". Biochim. Biophys. Acta. 1708 (1): 13–22. doi:10.1016/j.bbabio.2005.03.003. PMID 15949980.
  2. ^ Martin Engqvist; Maria Fabiana Drincovich; Ulf-Ingo Flügge & Veronica G. Maurino (2009). "Two D-2-hydroxyacid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and {beta}-oxidation pathways". J Biol Chem. 284 (September 11): 25026–25037. doi:10.1074/jbc.M109.021253. PMC 2757207. PMID 19586914.