Abstract
A soluble pyruvic dehydrogenase has been isolated from cell-free extracts of the H 37Ra strain of Mycobacterium tuberculosis var. hominis. Pyruvate is oxidatively decarboxylated to acetyl CoA and CO 2. Magnesium, DPN, CoA and DPT are required for this oxidation. The pyruvic dehydrogenase is inhibited by versene; magnesium can, in part, reverse this inhibition. K S values for DPN and CoA are 1.3·10 −5 and 5.5·10 −5 moles/liter, respectively. The pyruvic dehydrogenase appears to be part of an enzyme complex. Associated with the pyruvic dehydrogenase are a phosphotransacetylase, a lactic dehydrogenase and a lipoic dehydrogenase.
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