Abstract
Mutants resistant to the phenylalanine analogues o-fluoro-dl-phenylalanine (OFP) or p-fluoro-dl-phenylalanine (PFP) were isolated from a sake yeast, Saccharomyces cerevisiae Kyokai No. 9. They produced large amounts of β-phenylethyl alcohol and its acetate ester, which are rose-like flavor components. The tyrosine-dependent isozyme of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase (DAHP synthase; EC 4.1.2.15), in one of the OFP-resistant mutants was released from feedback inhibition by tyrosine. This mutant overproduced tyrosine in addition to β-phenylethyl alcohol and phenylalanine in minimal medium. In the PFP-resistant mutants, the activity of prephenate dehydrogenase (EC 1.3.1.12) was decreased to 5% of that in the wild type strain, while its DAHP synthase was increased four-fold. The tyrosine-dependent isozyme of this mutant was still sensitive to tyrosine. This mutant also overproduced tryptophan and phenylalanine in addition to β-phenylethyl alcohol in minimal medium.
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