暗紫贝母中法呢基焦磷酸合酶的生物信息学分析  

Bioinformatic Analysis of Farnesyl Pyrophosphate Synthase in Fritillaria unibracteata

作　　者：许勇[1] 李静 蔡标[1] 王红萍 戴陈伟 王娟 XU Yong;LI Jing;CAI Biao;WANG Hongping;DAI Chenwei;WANG Juan(Institute of Microbiology,Anhui Academy of Medical Sciences,Hefei 230061,China)

机构地区：[1]安徽省医学科学研究院微生物研究所,合肥230061

出　　处：《河南科学》2018年第7期1049-1055,共7页Henan Science

基　　金：安徽省"十三五"医疗卫生重点专科"病原微生物实验室"(皖卫科教[2017]30号);安徽省卫生计生委中医药科研课题"皖贝母内生真菌分离与鉴定"(2014zy46)

摘　　要：以暗紫贝母的法呢基焦磷酸合酶氨基酸序列为研究对象,利用CD search、ProtParam和SignalP等13种在线预测软件对其保守区域、理化性质、亚细胞定位、亲疏水性、二级结构、三级结构等性质进行分析.结果发现,该酶由352个氨基酸残基组成,是一种不含信号肽不跨膜、定位于线粒体基质的可溶性亲水蛋白,具有典型的类异戊二烯合成酶超家族结构域.其二级结构主要由α-螺旋和无规则卷曲组成.三级结构以PDB ID 4kk2.1为模板建模,包含两个聚异戊烯合酶位点,200 Lys为其结合配体Mg^(2+)的结合位点,活性区域由55个氨基酸残基构成,面积和体积分别为1 215.670?~2和1 496.051?~3.生物信息学手段分析预测结果揭示了暗紫贝母中法呢基焦磷酸合酶的性质、结构和功能,为进一步研究贝母活性生物碱的生物合成调控机制奠定理论基础.Using the amino acid sequence of farnesyl pyrophosphate synthase in Fritillaria unibracteata as the objects of this study,the conserved domains,physicochemical property,subcellular localization,hydrophobicity or hydrophilicity,secondary structure and tertiary structure were analyzed by 13 online prediction tools including CD search,ProtParam,SignalP and so on.The results showed that this enzyme,consisting of 352 amino acid residues,was an soluble hydrophilic protein in mitochondrial matrix without signal peptide and transmembrane structure.Alpha helix and random coil were main secondary structure components.The tertiary structure model was constructed with PDB ID 4kk2.1 as the template,and the 2 functional sites was polyisoprene synthase;the bingding site of Mg2+was 200 Lys;the active region was consisted of 55 amino acid residues,and the area and volume were 1 215.670?2 and 1 496.051?3.The characteristic,structure and function of the farnesyl pyrophosphate synthase in F.unibracteata were uncovered,which offered theoretical basis for the further study on regulatory mechanism of active alkaline biosynthesis in F.unibracteata.

关 键 词：暗紫贝母 法呢基焦磷酸合酶 生物碱 生物信息学 

分 类 号：R932[医药卫生—生药学] R318.04[医药卫生—药学]