类黄酮O-甲基转移酶(FOMT)的生物信息学分析

Bioinformatics Analysis of Flavonoid O-methyltransferase(FOMT)

类黄酮O-甲基转移酶(flavonoid O-methyltransferase,FOMT)是黄酮类化合物后修饰的关键酶,为进一步了解FOMT蛋白功能及特性,本研究采用生物信息学分析方法,对已在NCBI注册的50种FOMT蛋白的理化性质、蛋白质二、三级结构、信号肽等进行分析。结果表明,50种不同来源的FOMT氨基酸数目在186~391;蛋白分子量介于20.8~43.4 kD;理论等电点为4.82~6.37,均为酸性蛋白质;脂肪指数介于84.82~109.01;不稳定系数介于19.85~51.85,其中13种为稳定蛋白质,37种为不稳定蛋白质;亲疏水性分析显示,其中15种为疏水蛋白,25种为亲水蛋白。50种FOMT中仅有葛根来源的F3’-OMT含有跨膜结构,其余均为膜外蛋白。所有FOMT均属于AdoMet-MTase超家族蛋白。该结果以期为今后深入研究FOMT功能和甲基化黄酮类化合物的生物合成提供理论依据。

Flavonoid O-methyltransferase(flavonoid O-methyltransferase,FOMT)is the key enzyme in the post modification of flavonoids.In order to further understand the function and characteristics of FOMT,the physical and chemical properties,secondary and tertiary structures and signal peptides of 50 FOMT proteins registered in NCBI were analyzed by using bioinformatic method.The results showed that the number of FOMT amino acids from 50 different sources ranged from 186 to 391;the molecular weight of the protein ranged from 20.8 to 43.4 kD;the theoretical isoelectric point is 4.82~6.37,which are all acidic proteins;the fat index ranged from 84.82 to 109.01;the coefficient of instability ranged from 19.85 to 51.85,of which 13 were stable proteins and 37 were unstable proteins;hydrophobiciy analysis showed that 15 of them were hydrophobic proteins and 25 were hydrophilic proteins.Among the 50 FOMTs,only F3'-OMT from Pueraria lobata contains transmembrane structure,and the rest are extracellular proteins.All fomt belong to the AdoMet MTase superfamily.The results provide a theoretical basis for the further study of fomt function and biosynthesis of methylated flavonoids.