The potential binding interaction and hydrolytic mechanism of carbaryl with the novel esterase PchA in Pseudomonas sp. PS21
The potential binding interaction and hydrolytic mechanism of carbaryl with the novel esterase PchA in Pseudomonas sp. PS21
复制标题
西维因与假单胞菌中新型酯酶 PchA 的潜在结合相互作用和水解机制。
DOI：
10.1021/acs.jafc.1c06465
复制
发表时间：
2022
影响因子：
6.1
通讯作者：
Guohua Zhong
中科院分区：
文献类型：
--
作者：
Zhiyan Jiang;Liwen Qu;Gaopeng Song;Jie Liu;Guohua Zhong
微生物生物修复是缓解农业生态系统农药污染的有效途径，而水解酶是降解污染物的有效元素。在本研究中，从假单胞菌中鉴定出一种新型的依赖于Mn2+的酯酶PchA，它能有效地降解具有芳香族结构的氨基甲酸酯类农药。PS21。其水解性与核心催化结构域密切相关，核心催化结构域由6个残基组成。根据分子模拟阐明的结合模型，关键残基通过螯合Mn2+间接稳定了西维因的位置，西维因与几个疏水残基之间的额外疏水作用也稳定了结合构象。残基Glu398作为一般碱基，可以激活水分子，促进PchA催化。这项工作对西维因与水解酶PchA的结合作用和水解机理提供了有价值的见解，并将对设计能够降解相关污染物的蛋白质变体的策略至关重要。
Microbial bioremediation is a very potent and eco-friendly approach to alleviate pesticide pollution in agricultural ecosystems, and hydrolase is an effective element for contaminant degradation. In the present study, a novel Mn2+-dependent esterase, PchA, that efficiently hydrolyzes carbamate pesticides with aromatic structures was identified fromPseudomonassp. PS21. The hydrolytic activity was confirmed to be related closely to the core catalytic domain, which consists of six residues. The crucial residues indirectly stabilized the position of carbaryl via chelating Mn2+according to the binding model clarified by molecular simulations, and the additional hydrophobic interactions between carbaryl with several hydrophobic residues also stabilized the binding conformation. The residue Glu398, by serving as the general base, might activate a water molecule and facilitate PchA catalysis. This work offers valuable insights into the binding interaction and hydrolytic mechanism of carbaryl with the hydrolase PchA and will be crucial to designing strategies leading to the protein variants that are capable of degrading related contaminants.