Hui_2017_Acta.Crystallogr.F.Struct.Biol.Commun_73_515

Reference

Title : Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana - Hui_2017_Acta.Crystallogr.F.Struct.Biol.Commun_73_515
Author(s) : Hui R , Hu X , Liu W , Zheng Y , Chen Y , Guo RT , Jin J , Chen CC
Ref : Acta Crystallographica F Struct Biol Commun , 73 :515 , 2017
Abstract :

Zearalenone (ZEN) is a mycotoxin which causes huge economic losses in the food and animal feed industries. The lactonase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation of ZEN, is the only known ZEN-detoxifying enzyme. Here, a protein homologous to ZHD101, denoted CbZHD, from Cladophialophora batiana was expressed and characterized. Sequence alignment indicates that CbZHD possesses the same catalytic triad and ZEN-interacting residues as found in ZHD101. CbZHD exhibits optimal enzyme activity at 35 degrees C and pH 8, and is sensitive to heat treatment. The crystal structure of apo CbZHD was determined to 1.75 A resolution. The active-site compositions of CbZHD and ZHD101 were analyzed.

PubMedSearch : Hui_2017_Acta.Crystallogr.F.Struct.Biol.Commun_73_515
PubMedID: 28876230
Gene_locus related to this paper: xylba-a0a0d2h023

Related information

Substrate Zearalenone
Gene_locus xylba-a0a0d2h023
Family Zearalenone-hydrolase
Structure 5XWZ

Citations formats

Hui R, Hu X, Liu W, Zheng Y, Chen Y, Guo RT, Jin J, Chen CC (2017)
Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana
Acta Crystallographica F Struct Biol Commun 73 :515

Hui R, Hu X, Liu W, Zheng Y, Chen Y, Guo RT, Jin J, Chen CC (2017)
Acta Crystallographica F Struct Biol Commun 73 :515