不结球白菜BcGAPDH的生物信息学分析  

Bioinformatic Analysis of BcGAPDH from Brassica campestris ssp. chinensis

作　　者：马景蕃[1,2] 刘喜明[3] 陈小红[1,2] 

机构地区：[1]龙岩学院生命科学学院,福建龙岩364012 [2]福建省预防兽医学与兽医生物技术重点实验室,福建龙岩364012 [3]龙岩学院艺术与设计学院,福建龙岩364012

出　　处：《湖北农业科学》2016年第11期2917-2920,共4页Hubei Agricultural Sciences

基　　金：福建省科技厅重点项目(2012N0020);福建省教育厅A类项目(JA12320);国家自然科学基金培育项目(LG2014014)

摘　　要：采用生物信息学方法对克隆测序的不结球白菜(Brassica campestris ssp.chinensis)Bc GAPDH(3-磷酸甘油醛脱氢酶)蛋白质的理化性质、跨膜区、亲水性、亚细胞定位、所含模体及蛋白质结构进行了预测。理化性质分析表明,该酶含有328个氨基酸,相对分子量为35 161.2,p I值为9.03。TMpred跨膜分析表明,该酶没有跨膜螺旋区,这与Prot Scale预测的该酶为亲水性蛋白质相吻合。用Target P server程序预测该酶定位于线粒体上,结构域分析表明该酶含有多种磷酸化位点,二级结构以α-螺旋和随机卷曲为主。借助SWISS-MODEL软件对该酶进行了三维同源建模。The Bc GAPDH from Brassica campestris ssp. Chinensis was studied and its physical and chemical characters,transmembrane topologieal structure, hydrophily, subcellular localization, motif, secondary and tertiary structure of the protein were analyzed by bioinformation method. The results showed that the enzyme contained 328 amino acid residues, its molecular weight was 35 161.2, and the theoretical p I was 9.03. TMpred analysis showed that the enzyme didn＇t contain transmembrane helice which was overlap with the hydrophobic region that predicted by Prot Scale. It was located in mitochondria by Target P server. It contained many kinds of phosphorylation sites. Structure analysis showed that α-helix and random coil were the main secondary structures of this enzyme. In addition, the 3D model of Bc GAPDH was constructed.

关 键 词：不结球白菜(Brassica CAMPESTRIS ssp.chinensis) BC GAPDH 生物信息学 

分 类 号：S634.3[农业科学—蔬菜学]