The Chemical Structure of Tryptophanase from Escherichia coli
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منابع مشابه
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...
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...
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...
متن کاملA 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...
متن کاملSelection of mutants of Escherichia coli constitutive for tryptophanase.
Proc. Natl. Acad. Sci. U.S. 40:1064, 1954). The galactose mutations are of the same stability as the streptomycin-sensitivity gene. Some 60 other galactose mutants are similar to those reported in Table 1. No instances of mutability grossly higher than Gal16 or Galg have been noted, and no certain cases of failure to revert have been found. Combinations of Gal mutations have been synthesized vi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63063-7