圆弧青霉PG37脂肪酶的生物信息学分析

Bioinformatics Analysis of the Lipase from Penicillium cyclopium PG37

利用生物信息学软件对GenBank上登录的圆弧青霉PG37碱性脂肪酶(LipⅠ)进行预测和分析。结果表明,PG37LipⅠ全肽含多个疏水区域,无明显跨膜结构域,定位于胞外,N-末端20个氨基酸为信号肽;PG37LipⅠ成熟肽是等电点为6.16的疏水性稳定蛋白质,包含一个Lipase_3的结构域,属于α/β水解酶超家族,含磷酸化位点等多种功能性位点,具有脂肪酸代谢的功能;α-螺旋和不规则卷曲是其蛋白质二级结构的主要结构元件,在三级结构中,Ser132-Asp188-His2413个氨基酸残基组成酶活性中心。

The sequence of alkaline lipase （LipⅠ ）from Penicillium cyclopium PG37, registered in GenBank, was analyzed by bioinfnrmatics tools. The results showed that PG37 LipⅠ complete peptide that locates in ecto-cell features many hydrophobic regions and a signal peptide, but without transmembrane domain. PG37 Lip I is stable, pl 6. 16, with strong hydrophobicity, and contain one Li- pase_3 domain and is classified into α/β hydrolase superfamily. There are many phosphorylation sites and other functional sites in the sequence which involved in fatty acid metabolism, α-helix and random coil are the main secondary structures. Ser^132-Asp^188-His^341 compose the enzyme active region in the tertiary structure.