Summary: Acetolactate synthase from mitochondria of was markedly activated by ATP and feedback-inhibited by valine and, to a lesser extent, by other branched-chain amino acids. 2-Oxobutyrate, a substrate converted to acetohydroxybutyrate, had a much higher affinity for this enzyme than pyruvate and markedly inhibited the formation of acetolactate from pyruvate. The inhibition of growth of by threonine and the relief of this inhibition by valine are explained by these characteristic properties of acetolactate synthase, the key enzyme in the biosynthesis of branched-chain amino acids.


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