• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Structure >Coupling between catalytic site and collective dynamics: A requirement for mechanochemical activity of enzymes
【24h】

Coupling between catalytic site and collective dynamics: A requirement for mechanochemical activity of enzymes

机译：催化位点和集体动力学之间的耦合：酶的机械化学活性的要求

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

Growing evidence supports the view that enzymatic activity results from a subtle interplay between chemical kinetics and molecular motions. A systematic analysis is performed here to delineate the type and level of coupling between catalysis and conformational mechanics. The dynamics of a set of 98 enzymes representative of different EC classes are analyzed with the Gaussian network model (GNM) and compared with experimental data. In more than 70% of the examined enzymes, the global hinge centers predicted by the GNM are found to be colocalized with the catalytic sites experimentally identified. Low translational mobility (< 7%) is observed for the catalytic residues, consistent with the fine-tuned design of enzymes to achieve precise mechanochemical activities. Ligand binding sites, while closely neighboring catalytic sites, enjoy a moderate flexibility to accommodate the ligand binding. These findings could serve as additionalcriteria for assessing drug binding residues and could lessen the computational burden of substrate docking searches.
机译：越来越多的证据支持这样一种观点，即酶促活性是化学动力学和分子运动之间微妙的相互作用产生的。在这里进行了系统的分析，以描述催化和构象力学之间耦合的类型和水平。用高斯网络模型（GNM）分析了代表不同EC类的一组98种酶的动力学，并与实验数据进行了比较。在超过70％的检测酶中，发现GNM预测的全局铰链中心与实验确定的催化位点共定位。观察到催化残基的翻译移动性低（<7％），这与酶的微调设计相一致，以实现精确的机械化学活性。配体结合位点虽然紧邻催化位点，但具有适度的柔性以适应配体结合。这些发现可作为评估药物结合残基的附加标准，并可减轻底物对接搜索的计算负担。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
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