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Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli.

机译:腺苷3':5'-环一磷酸作为大肠杆菌中分解代谢物阻遏的介质。

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摘要

Measurements of intracellular adenosine 3':5'-cyclic monophosphate (cAMP) concentrations in E. coli under a variety of conditions show that levels of this nucleotide are well correlated with the rate of synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) in both catabolite repression and transient repression. These results, combined with extensive genetic and in vitro studies from a number of laboratories on the role of cAMP in E. coli, provide strong support for the concept that intracellular cAMP levels mediate the effects of catabolite and transient repression on rates on enzyme synthesis. Under all conditions studied, excretion can be described by a single rate constant, 2.1 min-1 at 37 degrees, indicating that intracellular levels cannot be regulated by alterations in the rate of cAMP excretion. Our data are fully consistent with the idea that carbon sources control intracellular cAMP levels by effects on its synthesis.
机译:在各种条件下对大肠杆菌中细胞内腺苷3':5'-环一磷酸(cAMP)浓度的测量表明,该核苷酸的水平与β-半乳糖苷酶(β-D-半乳糖苷半乳糖水解酶)的合成速率密切相关,EC 3.2.1.23)在分解代谢物抑制和瞬时抑制中均发挥作用。这些结果,再加上许多实验室对cAMP在大肠杆菌中的作用进行的广泛的遗传和体外研究,为细胞内cAMP水平介导分解代谢产物和瞬时抑制作用对酶合成速率的影响提供了强有力的支持。在研究的所有条件下,排泄都可以通过单一速率常数(37度下的2.1 min-1)来描述,这表明细胞内水平不能通过cAMP排泄速率的改变来调节。我们的数据与碳源通过影响其合成来控制细胞内cAMP水平的想法完全一致。

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