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圆弧青霉PG37脂肪酶的生物信息学分析
引用本文:李剑芳,张慧敏,邬敏辰.圆弧青霉PG37脂肪酶的生物信息学分析[J].生物技术通报,2010(3).
作者姓名:李剑芳  张慧敏  邬敏辰
作者单位:1. 江南大学食品学院,无锡,214122
2. 江南大学医药学院,无锡,214122
基金项目:国家自然科学基金项目 
摘    要: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。

关 键 词:生物信息学  圆弧青霉PG37  碱性脂肪酶  氨基酸序列

Bioinformatics Analysis of the Lipase from Penicillium cyclopium PG37
Li Jianfang,Zhang Huimin,Wu Minchen.Bioinformatics Analysis of the Lipase from Penicillium cyclopium PG37[J].Biotechnology Bulletin,2010(3).
Authors:Li Jianfang  Zhang Huimin  Wu Minchen
Institution:Li Jianfang1 Zhang Huimin1 Wu Minchen2(1 School of Food Science , Technology,Jiangnan University,Wuxi 214122,2 School of Medicine , Pharmaceutics,Wuxi 214122)
Abstract:The sequence of alkaline lipase (LipⅠ)from Penicillium cyclopium PG37,registered in GenBank,was analyzed by bioinformatics tools.The results showed that PG37 Lip I complete peptide that locates in ecto-cell features many hydrophobic regions and a signal peptide,but without transmembrane domain.PG37 Lip I is stable,pI 6.16,with strong hydrophobicity,and contain one Lipase_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~(241) compose the enzyme active region in the tertiary structure.
Keywords:Bioinformatics  Penicillium cyclopium PG37  Alkaline lipase  Amino acid sequence
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