Development of potent biocatalysts for enzymatic detoxification of estrogenic mycotoxin zearalenone (ZEN) and its more toxic derivative alpha-zearalenol (alpha-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 alpha-ZOL is then proposed. In addition, structure-based engineering to modify the substrate-binding pocket and improve the RmZHD activity toward alpha-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.
Zheng YY, Liu WT, Chen CC, Hu XY, Liu WD, Ko TP, Tang XK, Wei HL, Huang JW, Guo RT (2018) Crystal Structure of a Mycoestrogen-Detoxifying Lactonase from Rhinocladiella mackenziei: Molecular Insight into ZHD Substrate Selectivity ACS Catal8: 4294-4298
Zheng YY, Liu WT, Chen CC, Hu XY, Liu WD, Ko TP, Tang XK, Wei HL, Huang JW, Guo RT (2018) ACS Catal8: 4294-4298