%0 Journal Article
%T Functional Analysis of Trehalose Synthase in Meiothermus ruber CBS-01 by Site-directed Mutation<br>利用定点突变分析海藻糖合酶的功能
%A WANG Yu-Fan
%A ZHU Yue-Ming
%A WEI Dong-Sheng
%A ZHANG Jun
%A XING Lai-Jun
%A LI Ming-Chun
%A <br>王宇凡
%A 朱玥明
%A 魏东盛
%A 张 峻
%A 邢来君
%A 李明春
%J 微生物学通报
%D 2009
%I 
%X After constructed a 3D-Model and make the multiple sequence alignment of amino acid sequences of trehalose synthase from Meiothermus ruber CBS-01, we performed site-directed mutagenesis of D200G/H165R, R227C, R392A. And the ablity of convertion was detected. D200G/H165R and R392A lost their activities basically, while the ability of convertion of R227C declined at 50°C. When reacted at 37°C, D200G/H165R lost its activity, while R392A and R227C dropped their ability. At last, we found that R392 and D200 had important role on activity of enzyme, while R227 had little affection.
%K Trehalose synthase
%K Site-directed mutagenesis
%K Multiple sequence alignment
%K 3D-Model<br>海藻糖合酶
%K 定点突变
%K 序列比对
%K 三维模型构建
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=78024727B5F4EF6AA9CA8E605B5FC464&aid=85D8010BEF3AFF9334ED059CE76DF202&yid=DE12191FBD62783C&vid=933658645952ED9F&iid=94C357A881DFC066&sid=F86C3AE4543FDF24&eid=E7A4027472718CB3&journal_id=0253-2654&journal_name=微生物学通报&referenced_num=0&reference_num=13