Tsirul'nikov K B, Mel'nikov E E, Rotanova T V
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP Moscow, 117997 Russia.
Bioorg Khim. 2003 Sep-Oct;29(5):486-94. doi: 10.1023/a:1026049525351.
Regulation of activity of the proteolytic sites of Lon protease was studied. It was found that ATP-Mg has the properties of a noncompetitive activator of peptidase sites. The processive mechanism of the hydrolysis of protein substrates by Lon protease was experimentally confirmed under the conditions of ATP hydrolysis. It was shown that the oligomeric state of the enzyme is the necessary prerequisite for the processive proteolysis by the native Lon protease. The study of the properties of the mixed mutant Lon-K362Q/S679A confirmed the existence of the intra- and intersubunit pathways of signal transduction from the ATPase to proteolytic sites. The mutual influence of substrates of Lon protease was studied, and the existence of cooperative interactions between the peptidase sites in the oligomeric enzyme was suggested.
研究了Lon蛋白酶蛋白水解位点活性的调控。发现ATP-Mg具有肽酶位点非竞争性激活剂的特性。在ATP水解条件下，通过实验证实了Lon蛋白酶水解蛋白质底物的连续机制。结果表明，酶的寡聚状态是天然Lon蛋白酶进行连续蛋白水解的必要前提。对混合突变体Lon-K362Q/S679A特性的研究证实了从ATP酶到蛋白水解位点的亚基内和亚基间信号转导途径的存在。研究了Lon蛋白酶底物之间的相互影响，并提出寡聚酶中肽酶位点之间存在协同相互作用。
