Inhibiton by different amino acids of the aspartate kinase and the homoserine kinase of the yeastSaccharomyces cerevisiae

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Abstract
In this paper, we describe a simple method to measure the yeast homoserine kinase and asparate kinase activities, independently but in the same extract. With this method, we have determined some kinetic parameters for the physiological substrates of both enzymes, and investigated the inhibition exerted by different amino acids on these activities. Off all natural amino acids tested, only threonine inhibits effectively both enzymatic activities, although to a different degree. We did not find the reported inhibition by L‐homoserine over the asparate kinase. Altogether the data point to be asparate kinase and to the threonine as the key factors in the regulation of this route.