Mutations in Escherichia coli that Relieve Catabolite Repression of Tryptophanase Synthesis. Mutations Distant from the Tryptophanase Gene
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چکیده
منابع مشابه
Unstable mutations that relieve catabolite repression of tryptophanase synthesis by Escherichia coli.
From strains of Escherichia coli that carry deletions of the trp region, five different mutants were isolated that were capable of synthesizing tryptophanase at unusually high rates in conditions of severe catabolite repression. Notwithstanding the comparative insensitivity to catabolite repression, the rates of tryptophanase synthesis in the mutants were greatly diminished by the introduction ...
متن کاملMechanism of catabolite repression of tryptophanase synthesis in Escherichia coli.
Repression of tryptophanase (tryptophan indole-lyase) by glucose and its non-metabolizable analogue methyl alpha-glucoside has been studied employing a series of isogenic strains of Escherichia coli lacking cyclic AMP phosphodiesterase and altered for two of the proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), Enzyme I and Enzyme IIAGlc. Basal activity of tryptophanase...
متن کاملRepression of Tryptophanase Synthesis in Escherichia Coli.
Beggs, William H. (University of Cincinnati, Cincinnati, Ohio), and Herman C. Lichstein. Repression of tryptophanase synthesis in Escherichia coli. J. Bacteriol. 89:996-1004. 1965.-The nature of the glucose effect on tryptophanase in Escherichia coli (Crookes) was investigated to test the catabolite-repression hypothesis. Under static conditions of growth in the presence of 0.005 m glucose, try...
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The activity of the enzyme tryptophanase in the enteric environment was investigated to elucidate the significance of the enzyme in the metabolism of Escherichia coli. The tryptophanase activity, tryptophan content, and indole concentration as well as the numbers of E. coli were determined in the intestinal and fecal contents of conventional, germ-free, and monocontaminated axenic laboratory mi...
متن کاملEssential arginine residues in tryptophanase from Escherichia coli.
Tryptophanase from Escherichia coli B/1t7-A is inactivated by the arginine-specific reagent, phenylglyoxal, in potassium phosphate buffer at pH 7.8 AND 25 degrees. Apo- and holoenzyme are inactivated at the same rate, and inactivation of both is correlated with modification of 2 arginine residues/tryptophanase monomer. Substrate analogs having a carboxyl group protect the holoenzyme against bot...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1976
ISSN: 0022-1287
DOI: 10.1099/00221287-92-1-125