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Adenylate cyclase activity was measured in suspensions of E. coli B, rendered permeable with toluene. The enzyme was activated in a dose-dependent manner by GTP and by its non-hydrolysable analogue, GTP[γS]. In contrast, incubation with GDP[βS], a non-phosphorylatable analogue of GDP, caused a dose-related inhibition of adenylate cyclase; this was partially overcome by addition of GTP. GTP did not...
A mutant strain of Escherichia coli in which β-glucoside transport is resistant to catabolite inhibition by methyl α-glucoside was characterized. The mutation was probably within the gene, bglC, coding for the β-glucoside enzyme II. The mutant organism is shown to transport the β-glucoside substrate, salicin, in preference to methyl α-glucoside or fructose. Salicin also caused inducer exclusion of...
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