酶
化学
合理设计
催化作用
采样(信号处理)
蛋白质工程
生化工程
机制(生物学)
计算机科学
过渡(遗传学)
过渡状态
酶催化
组合化学
有机化学
纳米技术
材料科学
生物化学
工程类
物理
滤波器(信号处理)
计算机视觉
量子力学
基因
作者
Sree Ganesh Balasubramani,Kseniia Korchagina,Steven D. Schwartz
标识
DOI:10.1021/acs.jcim.4c00045
摘要
It is hoped that artificial enzymes designed in laboratories can be efficient alternatives to chemical catalysts that have been used to synthesize organic molecules. However, the design of artificial enzymes is challenging and requires a detailed molecular-level analysis to understand the mechanism they promote in order to design efficient variants. In this study, we computationally investigate the mechanism of proficient Morita-Baylis-Hillman enzymes developed using a combination of computational design and directed evolution. The powerful transition path sampling method coupled with in-depth post-processing analysis has been successfully used to elucidate the different chemical pathways, transition states, protein dynamics, and free energy barriers of reactions catalyzed by such laboratory-optimized enzymes. This research provides an explanation for how different chemical modifications in an enzyme affect its catalytic activity in ways that are not predictable by static design algorithms.
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