• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Catalysis science & technology >Insights into the enzymatic catalytic mechanism of bCinS: the importance of protein conformational change
【24h】

Insights into the enzymatic catalytic mechanism of bCinS: the importance of protein conformational change

机译：对BCIN的酶促催化机制的见解：蛋白质构象变化的重要性

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Although the available crystal structures of bCinS (Streptomyces clavuligerus 1,8-cineole synthase), a typical class I terpene cyclase (TPC), have shown notable protein conformational flexibility once bound with a substrate, the catalytic mechanism and the roles of protein conformational change are still unknown. Herein, we performed elaborate multiscale simulations to explore the detailed enzyme catalytic mechanism. The protein conformational change of the conserved kink region during catalytic processes and the ligand flexibility play important roles in regulating the catalytic selectivity of bCinS. Meanwhile, the importance of fleeting chiral intermediates is also discussed. Finally, the whole enzymatic cycle was concluded and the key structural factors (Mg2+ cations, R174 and G178) responsible for the active pocket conformational transformation from the “closed-A” to “closed-B” state were revealed. As a representative instance of enzymatic catalysis coupled with important protein conformational changes, it guides us to paying more attention on the potent catalytic roles of protein conformational change in other class I TPCs.
机译：尽管BCIN的可用晶体结构（链霉菌链霉菌1,8-核酸合酶），典型的I类萜烯环酶（TPC），显示出一旦与底物，催化机制和蛋白质构象变化的作用结合的明显蛋白质构象柔韧性仍然未知。本文中，我们进行了精心制作的多尺度模拟，以探索详细的酶催化机制。在催化过程中保守的扭结区域的蛋白质构象变化和配体柔韧性在调节BCIN的催化选择性方面起着重要作用。同时，还讨论了短暂的手性中间体的重要性。最后，结束了整个酶促周期，并揭示了从“闭合-A”到“封闭B”状态的主动口袋构象转换的关键结构因子（MG2+阳离子，R174和G178）。作为酶促催化的代表性实例，加上重要的蛋白质构象变化，它指导我们更多地注意其他I类TPC中蛋白质构象变化的有效催化作用。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号