SUMMARY: Acetohydroxyacid synthetase produced by 176 and a high penicillin-producing mutant have been compared. Both were sensitive to valine as the major feedback inhibitor. Inhibition of the enzyme in 176 appears to be effected through two valine binding sites, but only one of these remains in the high yielding strain and it is non-competitive with respect to pyruvate. The amount of enzyme activity detectable in the high yielding strain is more than twice the level in 176. Control of acetohydroxy-acid synthetase by other related amino acids was shown to be complex and involved sites other than the valine binding site.


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