蓝藻磷酸烯醇式丙酮酸羧化酶的生物信息学分析  

Bioinformatics Analysis on Phosphoenolpyruvate Carboxylase in Cyanobacteria

作　　者：侯李君[1] 王学魁[1] 施定基[1] 

机构地区：[1]天津科技大学海洋科学与工程学院,天津300457

出　　处：《生物技术通报》2008年第4期149-154,共6页Biotechnology Bulletin

基　　金：天津市科委重点攻关项目(043182711);国家自然科学基金资助(30670493);天津市高等学校科技发展基金项目(20040711)

摘　　要：应用NCBI、Expasy等在线生物信息学网站对蓝藻磷酸烯醇式丙酮酸羧化酶(PEPC)与其他物种进行序列同源比对,分析相同的保守序列及催化活性位点,构建分子进化树;预测跨膜结构、疏水性/亲水性、二级结构、功能域和模体等。结果显示,蓝藻PEPC与高等植物、细菌、真核藻PEPC同源性都比较低(约为33%),但是它们含有两个类似的活性部位和相同的催化活性位点;该蛋白质是非跨膜的亲水性不稳定蛋白,二级结构以a-螺旋和无规则卷曲为主,含有一个功能结构域,主要的功能是参与氨基酸的合成。The multi-sequence homological alignment of Phosphoenolpruvate Carboxylase between cyanobacteria and other species,the conservative sequence and catalyse active sites were analysed by online analysis at bioinformatics websites such as NCBI and Expasy. The phylogenetic tree was constructed by EBI ClustalW. The trans-membrane structure,hydrophobicity or hydrophilicity,secondary structure,functional domain and motifs of PEPC from cyanobacteria were predicted. The results showed that homologies between PEPC from cyanobacteria and those from bacteria,high plants and eukarya algae,were relative low （about 33%）.But they have similar active sites and identical active amino acids residue.The protein is a nontrans-membrane,hydrophilia and labile protein. Random coil and a-helix are the major secondary structure, It contains a functional domain,and main function is to synthesize amino acids.

关 键 词：磷酸烯醇式丙酮酸羧化酶 生物信息学 蓝藻(蓝细菌) 生物柴油 

分 类 号：Q946[生物学—植物学]