| Abstract |
The activity of acetohydroxy acid isomeroreductase, an essential enzyme for isoleucine and valine biosynthesis in Escherichia coli, was examined in a series of mutants containing derepressed levels of acetohydroxy acid synthetase activity but which differed from each other in the sensitivity of the synthetases to valine inhibition. The finding that isomeroreductase was highest in the strain with the synthetase that was least sensitive to valine inhibition supported the model of internal induction of the isomeroreductase by its acetohydroxy acid substrates. The mutation leading to the acetohydroxy acid synthetase least sensitive to valine was found to be unlinked to the ilv gene cluster and appeared to result in a synthetase that differed from the normal enzyme in several properties. The locus of this mutation is designated ilvF. The loci leading to derepression were designated azl. A pleiotropic, apparently single-step, mutation was found that led to restoration of end-product sensitivity to the synthetase, loss of end-product sensitivity of threonine deaminase [EC 4.2.1.16, l-threonine hydro-lyase (deaminating) and loss of isomeroreductase activity.
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