Characterization and catalytic mechanism of a direct demethylsulfide hydrolase for catabolism of the methylthiol-s-triazine prometryn

文献类型： 外文期刊

第一作者： Tang, Jun

作者： Tang, Jun;Yao, Jinjin;Pan, Dandan;Huang, Junwei;Wang, Jie;Wu, Xiangwei;Li, Qing X.;Dong, Fengshou

作者机构：

关键词： Prometryn; Triazine herbicide; Leucobacter triazinivorans JW-1; Biodegradation; Demethylthio

期刊名称：JOURNAL OF HAZARDOUS MATERIALS （ 影响因子：13.6； 五年影响因子：12.7 ）

ISSN： 0304-3894

年卷期： 2023 年 446 卷

页码：

收录情况： SCI

摘要： Demethylthio is one of the most important ways for microorganisms to metabolize triazine herbicides. Previous studies have found that the initial reaction of prometryn catabolism in Leucobacter triazinivorans JW-1 was the hydroxylation of its methylthio group, however, the corresponding functional enzyme was not yet clear. In this study, the gene proA was responsible for the initial step of prometryn catabolism from the strain JW-1 was cloned and expressed, and the purified amidohydrolases ProA have the ability to transform prometryn to 2-hydroxypro-pazine and methanethiol. The optimized reaction temperature and pH of ProA were 45 degrees C and 7.0, respectively, and the kinetic constants Km and Vmax of ProA for the catalysis of prometryn were 32.6 mu M and 0.09 mu mol/min/ mg, respectively. Molecular docking analyses revealed that different catalysis efficiency of ProA and TrzN (Nocardioides sp. C190) for prometryn and atrazine was due to non-covalent changes in amino acid residues. Our findings provide new insights into the understanding of s-triazine catabolism at the molecular level.

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