Reduction of 3-mercaptopyruvate in rat liver is catalyzed by lactate dehydrogenase.

It has been assumed that the in vivo reduction of 3-mercaptopyruvate, an intermediate of cysteine metabolism, to 3-mercaptolactate is catalyzed by lactate dehydrogenase (EC 1.1.1.27) though no definitive evidence has been presented. In order to examine this assumption, reduction of 3-mercaptopyruvate and its inhibition were studied using rat liver homogenate, lactate dehydrogenase purified from rat liver and anti-lactate dehydrogenase antiserum. Reduction of 3-mercaptopyruvate was actively catalyzed by rat liver homogenate and by the purified lactate dehydrogenase. This reducing activity was completely inhibited by anti-lactate dehydrogenase antiserum. These results indicate that the reduction of 3-mercaptopyruvate to 3-mercaptolactate in rat liver is catalyzed by lactate dehydrogenase.