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Stereochemistry of Pyruvate Kinase, Pyruvate Carboxylase, and Malate Enzyme Reactions

From the ¹ From The Institute for Cancer Research, Philadelphia, Pennsylvania 19111

Using isotopically asymmetric phosphoenolpyruvate-3-d,t it was established that pyruvate kinase causes the addition of a proton to C-3 from the face designated by a counterclockwise sequence of phosphate, carboxyl, and vinyl groups, the si face. Having shown that the pyruvate carboxylase reaction has a normal primary isotope effect, it was possible to determine its stereochemistry with enantiomorphic pyruvate prepared in the pyruvate kinase reaction. Carboxylation occurs with retention of configuration at carbon-3 of pyruvate. With this information, it was possible to analyze the enantiomorphic pyruvates formed by reaction of (3S)- or (3R)l-malate-3-d,t with malate enzyme. The decarboxylation occurred with retention.

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