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小单孢菌3’,4’-双脱羟基酶基因功能的研究

Function of 3′,4′-double dehydroxylase gene from Micromonospora

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【作者】 张国华洪文荣饶以群樊伟明朱宝泉

【Author】 ZHANG Guo-hua1,HONG Wen-rong1,RAO Yi-qun1,FAN Wei-ming2,ZHU Bao-quan3 1School of Biological Science and Technology,Fuzhou University,Fuzhou 350108;2Zhejiang Zhenyuan Pharmaceutical Co.Ltd.,Shaoxing 312000;3Shanghai Institute of Pharmaceutical Industry,Shanghai 200040,China

【机构】 福州大学生物科学与工程学院浙江震元制药有限公司上海医药工业研究院

【摘要】 根据文献查阅、同源比对及进化树分析,推测绛红色小单孢菌中gntI和伊纽小单孢菌sisI为3’,4’-双脱羟基酶基因。通过克隆得到gntI和sisI,随后将其构建到pET30a表达载体,并在E.coli BL21实现异源表达。利用生物信息学对该蛋白亲水性图谱、空间结构及活性域进行分析、预测。基于同源建模得到三级结构,推测其二级结构以α-螺旋为主,肽段40~60,100~120处可能为该酶活性中心。此研究为该酶进一步功能研究和应用奠定了基础。

【Abstract】 Through research in literature,homologous alignment and phylogenetic analysis,gntI from Micro-monospora purpurea and sisI from Micromonospora inyoensis were presumed to be 3′,4′-double dehydroxylase gene.Then the nucleic acid sequence of gntI and sisI were amplified and ligated to expression vector pET30 for heterologous expression in E.coli BL21.Bioinformatics was utilized to analyze the hydropathy plot,structure and catalytic domain of the protein GntI and sisI.Based on homologous modeling,the spatial structures were gained,speculating that α-helix was the main secondary structure,and catalytic domain may be located at 40-60,100-120 amino acids.This study established the foundation for further functional research and potential application of 3′,4′-double dehydroxylase.

【基金】 国家自然科学基金资助项目(No.31070093,No.30801449);国家“重大新药创制”科技重大专项资助项目(No.2009ZX09301-007);福建省教育厅科研基金资助项目(No.2007F5070)~~
  • 【文献出处】 中国药科大学学报 ,Journal of China Pharmaceutical University , 编辑部邮箱 ,2011年01期
  • 【分类号】Q753
  • 【被引频次】9
  • 【下载频次】187
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