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Review Article

丝氨酸/苏氨酸蛋白磷酸酶抑制剂：生化和结构研究为进一步发展提供了洞察力

卷 26, 期 15, 2019

页: [2634 - 2660] 页: 27

弟呕挨: 10.2174/0929867325666180508095242

价格: $65

摘要

背景：蛋白质的可逆磷酸化调节真核细胞中的许多关键功能。磷酸化由蛋白激酶催化，大部分磷酸化发生在丝氨酸和苏氨酸残基的侧链上。由蛋白激酶产生的磷酸单酯被蛋白磷酸酶水解。在没有磷酸酶的情况下，磷酸烷基二甲酯在25℃下水解的半衰期超过1万亿年; knon~2 x 10-20 sec-1。因此，ser / thr磷酸酶对可逆磷酸化控制的过程至关重要。 方法：本评价基于现有数据库中搜索的文献。我们比较了PPP家族磷酸酶（PPPase）的催化机制和靶向这些酶的抑制剂的相互作用。 结果：PPPase是金属依赖性水解酶，其将水解速率（[kcat / kM] / knon）提高~1021倍，使其成为地球上最强大的已知催化剂。生化和结构研究表明，通过10个保守氨基酸，DXH（X）~26DXXDR（X）〜20-26NH（X）~50H（X）~25-45R（X）~30，实现了PPP酶的显着催化效率。 -40H。六个作为金属配位残基。四个位置并定向基质磷酸盐。两个金属离子和10个催化残基一起定位磷酰基和活化的桥接水/氢氧化物亲核试剂，用于对基质磷原子的内联攻击。 PPPase在物种之间是保守的，并且许多结构上不同的天然毒素共同进化以靶向这些酶 结论：尽管催化位点是保守的，但是存在开发这种重要的金属酶组的选择性抑制剂的机会。

关键词: 磷酸酶，抑制剂，冈田酸，fostriecin，斑蝥素，tautomycin，microcystin晶体结构。

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