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In enzymology, a D-lactate dehydrogenase (cytochrome) () 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 . It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway ==References== * * * * Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「D-lactate dehydrogenase (cytochrome)」の詳細全文を読む スポンサード リンク
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