D-lactate dehydrogenase (cytochrome)
D-lactate dehydrogenase (cytochrome) | |||||||||
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Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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
pyruvate and ferrocytochrome c
.
This enzyme belongs to the family of
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
- 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. 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. PMID 13901630.
- Nygaard AP (1961). "D(−)-Lactate cytochrome c reductase, a flavoprotein from yeast". J. Biol. Chem. 236 (3): 920–925. PMID 13729965.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.