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大肠杆菌中磷酸转移酶系统对乳糖通透酶的调控机制:蛋白质-蛋白质相互作用的证据。

Mechanism of regulation of the lactose permease by the phosphotransferase system in Escherichia coli: evidence for protein-protein interaction.

作者信息

Osumi T, Saier M H

出版信息

Ann Microbiol (Paris). 1982 Mar-Apr;133(2):269-73.

PMID:7044217
Abstract

Binding of enzyme IIIglc to membranes was demonstrated in vitro, using membrane fragments from an E. coli strain which produces elevated levels of the lactose permease. Lactose and other substrates of the lactose permease enhanced the binding, but phosphoenolpyruvate decreased it in the presence of enzyme I and HPr. HPr also bound to the membranes under some conditions. The results support a model of permease regulation involving allosteric protein-protein interactions.

摘要

利用来自一株乳糖通透酶水平升高的大肠杆菌菌株的膜片段,在体外证明了酶IIIglc与膜的结合。乳糖和乳糖通透酶的其他底物增强了这种结合,但在酶I和HPr存在的情况下,磷酸烯醇丙酮酸会降低这种结合。在某些条件下,HPr也会与膜结合。这些结果支持了一种涉及变构蛋白-蛋白相互作用的通透酶调节模型。

相似文献

1
Mechanism of regulation of the lactose permease by the phosphotransferase system in Escherichia coli: evidence for protein-protein interaction.大肠杆菌中磷酸转移酶系统对乳糖通透酶的调控机制:蛋白质-蛋白质相互作用的证据。
Ann Microbiol (Paris). 1982 Mar-Apr;133(2):269-73.
2
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引用本文的文献

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Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography.X 射线晶体学揭示的麦芽糖转运蛋白的碳分解代谢物阻遏。
Nature. 2013 Jul 18;499(7458):364-8. doi: 10.1038/nature12232. Epub 2013 Jun 16.
3
Involvement of the central loop of the lactose permease of Escherichia coli in its allosteric regulation by the glucose-specific enzyme IIA of the phosphoenolpyruvate-dependent phosphotransferase system.
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4
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6
Cooperative binding of the sugar substrates and allosteric regulatory protein (enzyme IIIGlc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium.糖底物与变构调节蛋白(磷酸转移酶系统的酶IIIGlc)在大肠杆菌和鼠伤寒沙门氏菌中与乳糖和蜜二糖通透酶的协同结合。
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7
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