Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I.
Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I.
复制标题
大肠杆菌磷酸烯醇丙酮酸依赖性磷酸转移酶系统。
DOI:
10.1021/bi00546a009
复制
发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
G. Robillard
中科院分区:
文献类型:
--
作者:
O. Misset;M. Brouwer;G. Robillard
In vitro kinetic measurements have been performed by using purified HPr, EI, and a membrane fraction of EII from the Escherichia coli phosphoenolypyruvate-dependent sugar transport system. These measurements reveal very large lag times in the formation of methyl alpha-glucoside phosphate which are a function of the EI and the EII concentrations. The lag times decrease with increasing concentrations of EI but they increase with increasing concentrations of EII. When EI, together with Mg2+ and phosphoenolpyruvate, is preincubated at 37 degrees C before starting the kinetic measurements, the lag time can be decreased or eliminated. We have shown that the process responsible for the lag time is the activation of EI by dimerization which is influenced by Mg2+ and phosphoenolpyruvate.