The degradation of some Bz-substituted tryptophans by Escherichia coli tryptophanase
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چکیده
منابع مشابه
The degradation of some Bz-substituted tryptophans by Escherichia coli tryptophanase.
The present paper is the second in a series designed to correlate substrate structure with the kinetic constants of enzyme-catalysed reactions and thus throw light on the nature of the attachment of the substrate to the enzyme. Since the preparation of the first paper (Nath & Rydon, 1954), which describes the influence of structure on the hydrolysis of substituted phenylf-D-glucosides by emulsi...
متن کاملEscherichia 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 کاملAction of some substituted anthranilic acids on Escherichia coli.
Rydon (1) has found that 4and 5-methylanthranilic acids inhibit the growth of Eberthella typhi and that this inhibition is reversed by anthranilic acid, indole, and tryptophan. He concluded that the two methyl compounds interfere with the synthesis of tryptophan at the stage of anthranilic acid. Interruption in the conversion of anthranilic acid to indole in Escherichia coli, caused by chloromy...
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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1960
ISSN: 0306-3283
DOI: 10.1042/bj0740209