The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding
The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding
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DOI：
10.1002/1873-3468.14731
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发表时间：
2023-10-02
期刊：
影响因子：
3.5
通讯作者：
Owens，Cedric P.
中科院分区：
文献类型：
--
作者：
Omori，Kellie K.;Drucker，Charles T.;Owens，Cedric P.
绿原酸酯酶（Chlorogenic acid esterases，ChlE）是一类将绿原酸（Chlorogenic acid，CGA）水解成咖啡酸和奎尼酸的酶。ChlE可以分解食品中的CGA以改善其感官特性，并在消化系统中释放咖啡酸以改善生物活性化合物的吸收。本文报道了瑞士乳杆菌ChlE的结构、分子动力学和生化特性。分子动力学模拟表明，底物进入活性位点ofLhChlE是由两个发夹环以上的活性位点。对接模拟和突变分析表明，环内的两个残基，Gln145和Lys164，是重要的CGA结合。Lys164为CGA提供了轻微的底物偏好，而Gln145是有效周转所必需的。这项工作是第一次研究细菌叶绿素E的动力学，并提供了在这种类型的酶的底物结合偏好和营业额的见解。
Chlorogenic acid esterases (ChlEs) are a useful class of enzymes that hydrolyze chlorogenic acid (CGA) into caffeic and quinic acids. ChlEs can break down CGA in foods to improve their sensory properties and release caffeic acid in the digestive system to improve the absorption of bioactive compounds. This work presents the structure, molecular dynamics, and biochemical characterization of a ChlE fromLactobacillus helveticus(Lh). Molecular dynamics simulations suggest that substrate access to the active site ofLhChlE is modulated by two hairpin loops above the active site. Docking simulations and mutational analysis suggest that two residues within the loops, Gln145and Lys164, are important for CGA binding. Lys164provides a slight substrate preference for CGA, whereas Gln145is required for efficient turnover. This work is the first to examine the dynamics of a bacterial ChlE and provides insights on substrate binding preference and turnover in this type of enzyme.