不同丝状真菌Delta-12脱饱和酶的生物信息学比较分析

Bioinformatics analysis of Delta-12 desaturase in filamentous fungus

运用生物信息学方法对卷枝毛霉、稻根霉菌、高山被孢霉和米曲霉等丝状真菌的Delta-12脱饱和酶的氨基酸组成、理化性质、氨基酸保守位点、进化关系、信号肽、跨膜结构。亲水性/疏水性和二级结构等进行比较分析.结果表明:丝状真菌Detal-12脱饱和酶是一种亲水的稳定的膜结合蛋白,不具有信号肽,具有明显的疏水跨膜区域,有3个保守的His-box功能区域,二级结构主要由螺旋和不规则卷曲构成,其中螺旋占50%以上.

The research analyzed the compositions of amino acids, chemicophysical properties, conserved sequences, phylogenetic tree, signal peptides, trans - membrane regions, hydrophobicity, and secondary structure of Delta - 12 desaturase from filamentous fungus, including mucor. EIM - 10, Rhizopus oryzae, Mortierella alpine and AspergiUus oryzae. The results show that Delta- 12 desaturase is a stable hydrophilic membrane- binding protein, with non - signal peptide and transmembrane areas, three conservative functional domains of His - box. Helix and random coil are the main components of its secondary structure, and its helix is over 50%.