Title : Crystal Structure of a Mycoestrogen-Detoxifying Lactonase from Rhinocladiella mackenziei: Molecular Insight into ZHD Substrate Selectivity - Zheng_2018_ACS.Catal_8_4294 |
Author(s) : Zheng YY , Liu WT , Chen CC , Hu XY , Liu WD , Ko TP , Tang XK , Wei HL , Huang JW , Guo RT |
Ref : ACS Catal , 8 :4294 , 2018 |
Abstract :
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. |
PubMedSearch : Zheng_2018_ACS.Catal_8_4294 |
PubMedID: |
Gene_locus related to this paper: 9euro-a0a0d2ilk1 |
Substrate | Zearalenone Alpha-zearalenol |
Gene_locus | 9euro-a0a0d2ilk1 |
Structure | 5XO6 5XO7 5XO8 5Z5J 5Z7J 5Z97 |
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 Catal
8 :4294
Zheng YY, Liu WT, Chen CC, Hu XY, Liu WD, Ko TP, Tang XK, Wei HL, Huang JW, Guo RT (2018)
ACS Catal
8 :4294