Abstract
The regulatory properties of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DS) and chorismate mutase (CM) were compared between l-Trp-producing mutants and the wild-type strain of Bacillus subtilis K. The synthesis of DS in the l-Trp producers was elevated 6- to 13-fold compared to that in the wild-type strain, however, its synthesis was still repressed when the mutants were cultured in the presence of l-Phe and/or l-Tyr. The DS from the l-Trp-producers was still sensitive to inhibition by chorismate and prephenate. The specific activity of the CM in the l-Trp- producers was only 3% of that in the case of the wild-type strain, which was due to the loss of activity of the CM 1-type enzyme and which contributed to the derepression of DS and the higher l- Trp accumulation.
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