铜
多铜氧化酶
化学
漆酶
基质(水族馆)
酶
生物化学
生物
有机化学
生态学
作者
Li Xu,Zhiyi Wei,Zhang Min,Xiaohui Peng,Guangzhe Yu,Maikun Teng,Weimin Gong
标识
DOI:10.1016/j.bbrc.2006.12.116
摘要
CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.
科研通智能强力驱动
Strongly Powered by AbleSci AI