The Regulation of Isoleucine‐Valine Biosynthesis in Saccharomyces cerevisiae

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Abstract
Regulation of activity of acetohydroxyacid synthetase has been studied. L‐Valine, one of the end‐products of the combined pathway, is the only amino acid to inhibit strongly the enzyme (Ki= 5 × 10−5 M). Sensitivity to the inhibitor is rapidly lost by heating at 35°. The desensitized enzyme is stable at this temperature. In crude extracts, the enzyme is always partly desensitized, but 100% inhibition by valine is reached when the enzyme is assayed in situ, in benzene permeabilized cells. In addition, valine inhibition is more strictly dependent upon pH than activity itself. Kinetie studies of affinity for the substrate or inhibitor show no cooperative effects and valine inhibition seems truly competitive with pyruvate. Specific feedback inhibition by valine constitutes an additional proof that the acetohydroxyacid synthetase activity characterized in studies reported in the preceding paper, is operative for valine biosynthesis.

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