Crystal Structure of a Mycoestrogen-Detoxifying Lactonase from Rhinocladiella mackenziei: Molecular Insight into ZHD Substrate Selectivity
ACS Catalysis2018Vol. 8(5), pp. 4294–4298
Citations Over TimeTop 10% of 2018 papers
Yingying Zheng, Wenting Liu, Chun‐Chi Chen, Xiangying Hu, Weidong Liu, Tzu‐Ping Ko, Xueke Tang, Hongli Wei, Jian‐Wen Huang, Rey‐Ting Guo
Abstract
Development of potent biocatalysts for enzymatic detoxification of estrogenic mycotoxin zearalenone (ZEN) and its more toxic derivative α-zearalenol (α-ZOL) is of great interest. Here, we report the crystal structures of a ZEN-hydrolyzing enzyme from Rhinocladiella mackenziei (RmZHD), including substrate complexes. A molecular mechanism for the distinct activity of RmZHD in hydrolyzing the structurally similar ZEN and α-ZOL is then proposed. In addition, structure-based engineering to modify the substrate-binding pocket and improve the RmZHD activity toward α-ZOL is presented. These results expand our scope in understanding the catalytic mechanism of ZHD-family enzymes and are of vital importance in further industrial applications.
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