A Unified Mechanism Reveals the Evolutionary Origin of Enoyl Isomerases

• 全文链接

统一机制揭示烯酰异构酶的进化起源

关键词：

来源：

ACS Catalysis

全文链接：

//agri.nais.net.cn/topic/downloadFile/bf1583d3-ea72-4f38-953b-35294129db5d

来源地址：

https://pubs.acs.org/doi/10.1021/acscatal.5c05457

资源所属：

饲料用酶工程

类型：

学术文献

语种：

英语

原文发布日期：

2025-08-26

摘要：

Enoyl isomerases (EIs) and dehydratases (DHs) are critical for diversifying polyketide natural products; however, the underlying mechanism remains controversial. Through a combination of 1H NMR, solvent isotope effect (SIE) analyses, and mutagenesis applied to two bifunctional dehydratase/enoyl isomerases (DH/EIs), a “His-solo” monofunctional EI, and an engineered “Asp-solo” monofunctional EI, we uncovered a unified catalytic mechanism, highlighting the pivotal role of Asp-H2O in tuning the ratio of DH and EI activities. This mechanism not only deciphers the catalytic basis of these enzymes but also provides a comprehensive framework for understanding their evolutionary trajectory from DHs to DH/EIs and ultimately to EIs.