黄粉虫纤溶酶的三维结构模拟与序列分析  

Study on 3D-Structure Analogue and Sequence Analysis of Fibrinolysin from Tenebrio Molitor

作　　者：余磊[1] 韩雅莉[2] 

机构地区：[1]武汉软件工程职业学院,湖北武汉430205 [2]广东工业大学,广东广州510006

出　　处：《化学与生物工程》2013年第9期32-34,50,共4页Chemistry & Bioengineering

基　　金：国家自然科学基金资助项目(30772739)

摘　　要：为了深入研究黄粉虫纤溶酶的纤溶机理,用生物信息学方法对黄粉虫纤溶酶进行了三维结构模拟与序列分析。首先找到了其活性中心,利用Biosun软件的同源模建技术,模拟了黄粉虫纤溶酶的三维结构;利用Goldkey软件,对黄粉虫纤溶酶的氨基酸序列进行了分析,重点讨论了其等电点、亲水性、柔性与催化活性之间的关系,最后对纤维蛋白水解部位结构进行了分析。结果表明,黄粉虫纤溶酶的活性中心是组氨酸、丝氨酸和天冬氨酸三个氨基酸残基,位于球蛋白中心凹穴处,底物结合部位是丝氨酸、天冬氨酸和甘氨酸。从微观分子水平上阐述了该类酶水解纤维蛋白的机理是催化精氨酸-赖氨酸肽键水解,与报道的纤维蛋白的溶解机理相符。In order to further study on the mechanism of fibrinolysin from Tenebrio molitor, the 3D-structure of the enzyme was simulated, while the isoelectric point, hydrophilicity, and flexibility of the sequences were analyzed, using bioinformatics methods. The active sites of the enzyme were histidine, serine and aspartic acid in the center of globin cavity,while the substrate binding sites were serine,aspartic acid and glycine. The fibrinolysin＇s catalytic mechanism was catalyzing hydrolysis of the peptide bonds between arginine and lysine.

关 键 词：黄粉虫 纤溶酶 三维结构 序列 

分 类 号：Q556.3[生物学—生物化学]