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Studies on the decarbosylation of pyruvate. II. Kinetic studies on the binding of thiamine pyrophosphate to pyruvate decarboxylase.

The reconstitution of pyruvate decarboxylase has been studied kinetically in thepresence of several concentrations of thiamine pyrophosphate (TPP) and Mn2+. The Km for TPP determined graphically was decreased by increasing Mn2+ concentration, while Vmax was almost unchanged. The values of Kms for Mn2+ and Vmax, were affected in mixed manner by the amount of TPP.The significance of Kms thus determined is discussed and the values are compared to that determined in transketolase.