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- W1803665384 abstract "4-Fluorophenylalanine-resistant mutants of Salmonella typhimurium were isolated in which tyrosine pathway enzymes were not repressed by l -tyrosine. The mutants produced elevated levels of 3-deoxy- d -arabinoheptulosonic acid 7-phosphate (DAHP) synthetase (tyr) and chorismate mutase T-prephenate dehydrogenase, and these enzymes as well as transaminase A were not repressed by high concentrations of tyrosine. Genetic analysis revealed that a mutation in a gene designated tyrR was responsible for the constitutivity of the tyrosine pathway enzymes in strains SG1, SG7, and SG9, and that tyrR was linked to pyrF . In strain SG1 a mutation had also occurred in aroF , the structural gene for DAHP synthetase (tyr), resulting in loss of sensitivity of this enzyme to end-product inhibition. There appeared to be no relationship between loss of feedback inhibition and loss of end-product repression, since derivative strains of SG1 that carried only the tyrR mutation behaved like the singly mutated tyrR strains, SG7 and SG9, in showing high constitutive levels of tyrosine-specific enzymes that were not repressed by tyrosine." @default.
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- W1803665384 date "1973-09-01" @default.
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- W1803665384 title "tyrR, A Regulatory Gene of Tyrosine Biosynthesis in Salmonella typhimurium" @default.
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- W1803665384 doi "https://doi.org/10.1128/jb.115.3.1094-1102.1973" @default.
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