Seok Y J, Koo B M, Sondej M, Peterkofsky A
School of Biological Sciences, Seoul National University, Korea.
J Mol Microbiol Biotechnol. 2001 Jul;3(3):385-93.
Bacteria sense continuous changes in their environment and adapt metabolically to effectively compete with other organisms for limiting nutrients. One system which plays an important part in this adaptation response is the phosphoenol-pyruvate:sugar phosphotransferase system (PTS). Many proteins interact with and are regulated by PTS components in bacteria. Here we review the interaction with and allosteric regulation of Escherichia coli glycogen phosphorylase (GP) activity by the histidine phosphocarrier protein HPr, which acts as part of a phosphoryl shuttle between enzyme I and sugar-specific proteins of the PTS. HPr mediates crosstalk between PTS sugar uptake and glycogen breakdown. The evolution of the allosteric regulation of E. coli GP by HPr is compared to that of other phosphorylases.
细菌感知其环境中的持续变化，并进行代谢适应，以便与其他生物有效竞争有限的营养物质。在这种适应性反应中起重要作用的一个系统是磷酸烯醇丙酮酸：糖磷酸转移酶系统（PTS）。在细菌中，许多蛋白质与PTS组分相互作用并受其调节。在这里，我们综述了组氨酸磷酸载体蛋白HPr对大肠杆菌糖原磷酸化酶（GP）活性的相互作用和变构调节，HPr作为PTS中酶I和糖特异性蛋白之间磷酸化穿梭的一部分发挥作用。HPr介导了PTS糖摄取与糖原分解之间的串扰。将HPr对大肠杆菌GP变构调节的进化与其他磷酸化酶的进化进行了比较。
