Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies.
Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies.
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大肠杆菌 ATP 依赖性 Lon 蛋白酶机械酶学的最新进展：动力学研究的亮点。
DOI：
10.1039/b609936j
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发表时间：
2006
影响因子：
--
通讯作者：
Suzuki,CarolynK
中科院分区：
文献类型：
--
作者：
Lee,Irene;Berdis,AnthonyJ;Suzuki,CarolynK
Lon protease, also known as protease La, is one of the simplest ATP-dependent proteases that plays vital roles in maintaining cellular functions by selectively eliminating misfolded, damaged and certain short-lived regulatory proteins. Although Lon is a homo-oligomer, each subunit of Lon contains both an ATPase and a protease active site. This relatively simple architecture compared to other hetero-oligomeric ATP-dependent proteases such as the proteasome makes Lon a useful paradigm for studying the mechanism of ATP-dependent proteolysis. In this article, we survey some recent developments in the mechanistic characterization of Lon with an emphasis on the utilization of pre-steady-state enzyme kinetic techniques to determine the timing of the ATPase and peptidase activities of the enzyme.
