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Abstract
The reaction catalyzed by crystalline yeast phosphoglyceric acid mutase is inhibited by the substrate (d-2-phosphoglyceric acid). In order to elucidate the mechanism of this substrate inhibition, detailed investigations have been performed. It is proved that the substrate inhibition in this enzyme reaction is caused by the facts that the coenzyme-binding site on the enzyme is covered by the substrate and the combination of the coenzyme with the enzyme is interfered by the substrate. Consequently, it is concluded that the substrate is a competitive inhibitor of the coenzyme.
Abstract
Various compounds reveal the inhibitory actions for yeast phosphoglyceric acid mutase. In order to clarify the mechanism of this enzyme reaction, it is necessary to understand the behaviors of the inhibitors in relation to the unavoidable substrate inhibition. According to the result, it is confirmed that Zn++ and pyrophosphate are competitive inhibitors of the coenzyme. Moreover, the mechanism of the fluoride inhibition has been investigated under the several conditions in detail.
Abstract
Crystalline yeast phosphoglyceric acid mutase is composed of several components electropho-retically and these components have the different specific activities. Therefore, in order to study the differences among the individual components, it is necessary to isolate each component in a large quantity. For this purpose, the special vertical zone electrophoresis apparatus with Hg-Hg2Cl2 reversible electrodes has been constructed and by using it a large amount of each component has been separated. Moreover, each component separated has been crystallized. The crystalline forms of the individual components are the same.