来自班替枝孢霉的一种新型玉米赤霉烯酮水解酶的表征及晶体结构
Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana.
作者信息
Hui Renjie, Hu Xiangying, Liu Wenting, Liu Weidong, Zheng Yingying, Chen Yun, Guo Rey Ting, Jin Jian, Chen Chun Chi
机构信息
School of Pharmaceutical Sciences, Jiangnan University, 1800 Lihu Avenue, Binhu District, Wuxi, Jiangsu 214122, People's Republic of China.
School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Binhu District, Wuxi, Jiangsu 214122, People's Republic of China.
出版信息
Acta Crystallogr F Struct Biol Commun. 2017 Sep 1;73(Pt 9):515-519. doi: 10.1107/S2053230X17011840. Epub 2017 Aug 21.
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°C and pH 8, and is sensitive to heat treatment. The crystal structure of apo CbZHD was determined to 1.75 Å resolution. The active-site compositions of CbZHD and ZHD101 were analyzed.
摘要
玉米赤霉烯酮（ZEN）是一种霉菌毒素，在食品和动物饲料行业造成巨大经济损失。来自粉红粘帚霉的内酯酶ZHD101可催化ZEN的水解降解，是唯一已知的ZEN解毒酶。在此，表达并表征了来自茄病镰刀菌的与ZHD101同源的蛋白质CbZHD。序列比对表明，CbZHD具有与ZHD101相同的催化三联体和与ZEN相互作用的残基。CbZHD在35°C和pH 8时表现出最佳酶活性，并且对热处理敏感。测定了无配体CbZHD的晶体结构，分辨率为1.75 Å。分析了CbZHD和ZHD101的活性位点组成。
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