醛脱氢酶(ALDH)蛋白家族的信息学比较分析与修饰预测  

Comparative Analysis and Mutation Prediction of Aldehyde Dehydrogenase Based on the Bioinformatics Methods

作　　者：常凯[1] 童立冬 江忠勇[1] 熊怡淞[1] 张睿[1] 熊杰[1] 

机构地区：[1]中国人民解放军成都军区总医院检验科,成都610083 [2]中国人民解放军成都军区总医院放射科,成都610083

出　　处：《基因组学与应用生物学》2016年第1期28-33,共6页Genomics and Applied Biology

基　　金：四川省科技厅应用基础研究项目(2013JY0173)基金资助

摘　　要：以ALDH1~ALDH4为核心,利用生物信息学方法对比分析ALDH家族成员的蛋白理化性质、亚细胞定位、构建分析蛋白三维模型并绘制家族系统进化树。对不稳定蛋白进行修饰预测。结果表明：ALDH家族间的序列相似性较高但同源性相对较低,氨基酸序列差异较大。蛋白的GRAVY值（-0.284~0.01）和分子量（47 974.0~61 810.5）没有典型的规律性分布,但不稳定指数、脂肪系数和等电点差异显著。结构分析催化位点和结合区域有较大差异,这赋予了各家族成员不同的催化活性。最后就不稳定蛋白进行了理想的模拟突变与预测分析。分析结果可为ALDH蛋白的研究提供有价值信息,为进一步研究ALDH在人体内的疾病发生途径与作用机理提供依据。In order to modify and predict the unstable protein, the physical and chemical properties of protein and subcellular localization were analyzed, and the tertiary structure of protein was built and analyzed, then the phylogenetic tree of the ALDH family was drew by using bioinformatics methods, which was in the center of ALDH1-ALDH4. The result showed that the similarity was higher but the homology was relatively low among the sequence of ALDH family, while acid sequence had more difference. There was no special regularity of the distribution in GRAVY values （-0.284-0.01） and molecular weight of protein （47 974.0-61 810.5）, but instability index, aliphatic index and isoelectric point were significantly different. Catalytic site and binding domain were analyzed to have more differences, which gave different catalytic activity to members in every family. At last, the stability of unstable protein was predicted after modification. The results of the analysis might provide valuable information for the study of ALDH protein, and provide the basis for further study of the ways and the mechanism of ALDH on how it works in human body.

关 键 词：醛脱氢酶 生物信息学 对比分析 蛋白特征 修饰预测 

分 类 号：Q55[生物学—生物化学]