Escherichia coli Tryptophanase in the Enteric Environment

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Escherichia coli tryptophanase in the enteric environment.

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...

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Repression 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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Essential 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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A structural view of the dissociation of Escherichia coli tryptophanase.

Tryptophanase (Trpase) is a pyridoxal 5'-phosphate (PLP)-dependent homotetrameric enzyme which catalyzes the degradation of L-tryptophan. Trpase is also known for its cold lability, which is a reversible loss of activity at low temperature (2°C) that is associated with the dissociation of the tetramer. Escherichia coli Trpase dissociates into dimers, while Proteus vulgaris Trpase dissociates in...

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Isolation of Mutants Affecting Tryptophanase Production in Escherichia Coli.

Gartner, Theodore K. (University of California, Davis), and Monica Riley. Isolation of mutants affecting tryptophanase production in Escherichia coli. J. Bacteriol. 89:313-318. 1965.-Mutants of Escherichia coli K-12 were isolated which appear to have suffered an alteration in the regulation system governing tryptophanase synthesis. A novel selection method was used to isolate tryptophanase muta...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1972

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.109.1.74-80.1972