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J. Biochem, 1978, Vol. 83, No. 3 879-886
© 1978 Japanese Biochemical Society


research-article

Altered Regulatory Mechanisms for Tryptophan Synthesis in Fluorotrptophan-Resistant Mutants of Brevibacterium flavum

Isamu SHIIO and Shin-ichi SUGIMOTO

Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki-ku Kawasaki, Kanagawa 210

5-Fluorotryptophan (5FT) inhibited the activity of anthranilate synthetase (AS) of Brevi-bacterium flavum as strongly as did tryptophan. The concentration of 5FT required for complete inhibition of AS was similar to that for growth inhibition. Higher concentrations of 5FT repressed the synthesis of the tryptophan enzymes with a non-coordinate relationship between AS or anthranilate-phosphoribosylpyrophosphate phosphoribosylransferase (PRT) and indole-3-glycerol phosphate synthetase (InGPS) or tryptophan synthetase (TS)-B. In a mutant resistant to low concentrations of 5FT, strain 251, which produced anthranilate and had an AS less sensitive to feedback inhibition by tryptophan, all the tryptophan enzymes showed normal levels. On the other hand, in a mutant resistant to higher concentrations of 5FT, which was derived from strain 251 and produced L-tryptophan, the synthesis of all the tryptophan enzymes except PRT had been derepressed. In mutants resistant to high concentrations of 5FT, strains 1288 and 399, which were derived directly from the wild-type strain and produced L-tryptophan, the syntheses of all the tryptophan enzymes and of all except TS had been derepressed, respectively, in addition to desensitization of AS to feedback inhibition. From these results, it was concluded that the syntheses of the five enzymes in the tryptophan pathway are regulated independently of each other in B. flavum and that derepression of PRAI and of InGPS, as well as desensitization of AS to feedback inhibition, is essential for tryptophan overproduction. Among L-tryptophan-producing mutants, the amount of L-tryptophan produced depended on the extent of desensitization of AS rather than the specific activities of the derepressed enzymes.


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