• 新闻与活动

    学术成果

Understanding the entropic effect in chorismate mutase reaction catalyzed by isochorismate-pyruvate lyase from Pseudomonas aeruginosa (PchB)†

Catal. Sci. Technol.,2019,9, 957-965

Elucidation of the role of entropy in enzymatic reactions can be utilized in the de novo design of enzymes or protein engineering. Recently, the change in entropy in the enzyme-catalyzed chorismate mutase reaction brought about uncertainty as a result of an experiment using PchB, in which the measured change in entropy was comparable to the reported value for the uncatalyzed reaction in an aqueous solution, which contrasted with the general proposed entropy-driven mechanism. On the basis of a sufficient sample from quantum mechanics/molecular mechanics molecular dynamics simulations, the entropic effect in the PchB-catalyzed chorismate mutase reaction has been determined for the first time. Calculations suggest that the PchB-catalyzed chorismate mutase reaction is entropy-driven. An additional entropic penalty was revealed from the substrate preorganization process, which led to a remarkable apparent entropic effect in the reaction. Our findings provide an explanation of the uncertainty regarding the large measured entropic effect in experiments and confirm the entropy-driven character of the PchB-catalyzed chorismate mutase reaction. The clarification of the change in entropy in this enzymatic reaction would provide useful clues for future enzyme design projects.

想继续了解更多?

联系我们

我们期待您的留言

让我们知道如何为您提供帮助,我们团队将24小时内与您联系!

姓名
电话
邮箱
国家/地区
北京市
天津市
上海市
重庆市
河北省
山西省
辽宁省
吉林省
黑龙江省
江苏省
浙江省
安徽省
福建省
江西省
山东省
河南省
湖北省
湖南省
广东省
海南省
四川省
贵州省
云南省
陕西省
甘肃省
青海省
台湾省
内蒙古自治区
广西壮族自治区
西藏自治区
宁夏回族自治区
新疆维吾尔自治区
香港特别行政区
澳门特别行政区
从事行业
小分子药物研发
抗体药物研发
CRO/CDMO
投融资机构
高校/研究院所/医院
园区
生物医药产业
感兴趣的业务
小分子药物发现
抗体药物发现
药物固体形态研发
化学合成服务(含自动化合成)
实验室自动化解决方案
所在公司
是否需要业务人员跟进?
暂不需要
验证码

我已阅读并同意 晶泰科技隐私政策法律声明