D-lactate dehydrogenase (cytochrome)

D-lactate dehydrogenase (cytochrome)
D-lactate dehydrogenase (cytochrome)
EC number
CAS number 37250-79-6
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

(D)-lactate + 2 ferricytochrome c \rightleftharpoons 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


  • GREGOLIN C, SINGER TP (1963). "The lactic dehydrogenase of yeast. III. D(-)Lactic cytochrome c reductase, a zinc-flavoprotein from aerobic yeast". Biochim. Biophys. Acta. 67: 201–18. doi:10.1016/0006-3002(63)91818-3. PMID 13950255. 
  • GREGOLIN C, SINGER TP, KEARNEY EB, BOERI E (1961). "The formation and enzymatic properties of the various lactic dehydrogenases of yeast". Ann. N. Y. Acad. Sci. 94 (3): 780–97. doi:10.1111/j.1749-6632.1961.tb35573.x. PMID 13901630. 
  • Nygaard AP (1961). "D(-)-Lactate cytochrome c reductase, a flavoprotein from yeast". J. Biol. Chem. 236: 920–925. 
  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.