Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference41 articles.
1. New insight into the catalytic mechanism of chorismate mutases from structural studies
2. Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate
3. An inhibitor of chorismate mutase resembling the transition-state conformation
Cited by 98 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. On the Importance of Preserving Active Induced-Fit Conformations during Enzyme-Catalyzed Reactions: a Case Study of CARNMT1;2024-07-18
2. Kinetic View of Enzyme Catalysis from Enhanced Sampling QM/MM Simulations;Journal of Chemical Information and Modeling;2024-04-12
3. Best Practices on QM/MM Simulations of Biological Systems;Journal of Chemical Information and Modeling;2023-04-26
4. Evaluating the active site-substrate interplay between x-ray crystal structure and molecular dynamics in chorismate mutase;The Journal of Chemical Physics;2023-02-09
5. Structural and Energetic Origin of Different Product Specificities and Activities for SETD3 and Its Mutants on the Methylation of the β-Actin H73K Peptide: Insights from a QM/MM Study;Journal of Chemical Theory and Computation;2022-12-15
1.学者识别学者识别
2.学术分析学术分析
3.人才评估人才评估
"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370
www.globalauthorid.com
TOP
Copyright © 2019-2024 北京同舟云网络信息技术有限公司 京公网安备11010802033243号 京ICP备18003416号-3