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Catalytic inactivation of alkaline phosphatase by cantharidin, an inhibitor of protein phosphatase

机译：蛋白磷酸酶抑制剂cantharidin催化灭活碱性磷酸酶

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Previous investigations have shown high toxicity of cantharidin to many insects especially lepidopteran. However, its use in a higher dose for pest management has raised serious environmental concerns. Therefore, its biological potential in sub-lethal dose as a synergist was considered. It is essential for a synergist to be an effective inhibitor of metabolic enzymes, especially those responsible for biotic and abiotic stresses. As alkaline phosphatases are an important type of enzyme involved in numerous physiological processes and also in insecticide resistance, any impairment in their function may lead to serious physiological disturbances and could compromise their catalytic activity. Results showed that a sub-lethal dose of 25 mu g g-1 treated artificial diet fed to Helicoverpa armigera showed inhibitory effects on catalytic activity of alkaline phosphatase in the insect midgut. Furthermore, kinetic data showed that cantharidin inhibited HaALPs competitively with respect to p-NPP. The inhibitory effect of cantharidin on the catalytic activity of ALPs as a result of its binding to the putative catalytic site was also confirmed by using homology modelling, molecular dynamics and docking simulations.
机译：先前的研究表明，th藤素对许多昆虫特别是鳞翅目昆虫具有高毒性。但是，以更高剂量用于害虫管理已引起严重的环境问题。因此，考虑了其在亚致死剂量下作为增效剂的生物学潜力。增效剂必须是代谢酶的有效抑制剂，尤其是那些负责生物和非生物胁迫的酶。由于碱性磷酸酶是参与许多生理过程以及杀虫剂抗性的一种重要酶，因此其功能的任何损害都可能导致严重的生理紊乱并可能损害其催化活性。结果表明，亚致死剂量的25μg g-1处理过的人工饲料饲喂棉铃虫，对昆虫中肠中碱性磷酸酶的催化​​活性具有抑制作用。此外，动力学数据表明，相对于p-NPP，斑th素具有竞争性抑制HaALP的作用。通过使用同源性建模，分子动力学和对接模拟，也证实了鸟th素由于与假定的催化位点结合而对ALPs催化活性的抑制作用。

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