Abstract
Crystalline phosphoglyceric acid mutase preparations obtained from autolyzate of baker's yeast contain five components which are electrophoretically distinguishable and which exhibit different specific activities. These components are not isozymes. One of these components is the native protein (component I) and the others arise from the action of PGA mutase-modifying enzyme during autolysis. The enzyme which modifies native PGA mutase to produce components (II, III, IV, and V) with higher electrophoretic mobilities and lower specific activities than the native enzyme has been shown to be a peptide hydrolase. Quantitative measurements have indicated that amino acids (lysine, asparagine, glutamine, alanine, valine, and glycine) are liberated during the conversion of component I to the limit product (component V). It has been shown that electrophoretic mobilities of the modified components correlate with the liberation of lysine. Major conformational changes have not been observed during the modification. Some properties of the modifying enzyme, and of component I and V of PGA mutase are presented.
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