文献类型：期刊文献

英文题名：Molecular dynamics investigation of the interaction between Colletotrichum capsici cutinase and berberine suggested a mechanism for reduced enzyme activity

作者：Li, Ying[1];Wei, Jinqing[1];Yang, Huizhen[1];Dai, Jing[2];Ge, Xizhen[1]

第一作者：李映

通讯作者：Ge, XZ[1]

机构：[1]Beijing Union Univ, Coll Biochem Engn, Beijing Key Lab Biomass Waste Resource Utilizat, Beijing, Peoples R China;[2]Beijing Aerosp Petrochem EC & EP Technol Co Ltd, Beijing, Peoples R China

第一机构：北京联合大学生物化学工程学院

通讯机构：[1]corresponding author), Beijing Union Univ, Coll Biochem Engn, Beijing Key Lab Biomass Waste Resource Utilizat, Beijing, Peoples R China.|[1141726]北京联合大学生物化学工程学院;[11417]北京联合大学;

年份：2021

卷号：16

期号：2

外文期刊名：PLOS ONE

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000620629200026)】；

基金：Ying Li and Xizhen Ge received funding from Beijing Municipal Commission of Education [KZ201911417049]; Special Project of Major Science and Technology of Hebei Province [19026517Z]; Beijing Municipal Education Commission Technology Plan [KM202011417006]. The funders only provided financial support in the form of research materials while had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Mrs Jing Dai is a staff of the commercial company 'Beijing Aerospace Petrochemical EC&EP Technology Co., Ltd'. This company only provided salaries for Mrs Jing Dai.

语种：英文

摘要：Berberine is a promising botanical pesticide against fungal plant pathogens. However, whether berberine inhibits the invasion of fungal pathogen across plant surface remains unclear. Here we demonstrated that the enzyme activities of purified cutinase from fungal pathogen Colletotrichum capsici were partially inhibited in presence of berberine toward different substrates. Molecular dynamics simulation results suggested the rigidity of cutinase was decreased with berberine added into the system. Interestingly, aggregations of berberine to the catalytic center of cutinase were observed, and stronger hydrophobic interactions were detected between key residue His 208 and berberine with concentrations of berberine increased. More importantly, this hydrophobic interaction conferred conformational change of the imidazole ring of His 208, which swung out of the catalytic center to an inactive mode. In summary, we provided the molecular mechanism of the effect of berberine on cutinase from C. capsici.