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植物研究 ›› 2010, Vol. 30 ›› Issue (3): 337-343.doi: 10.7525/j.issn.1673-5102.2010.03.015

• 论文 • 上一篇    下一篇

植物Δ12-脂肪酸脱氢酶的生物信息学分析

刘万宏;朱蠡庆;姚波   

  1. 重庆科技学院生物系,重庆 401331
  • 收稿日期:1900-01-01 修回日期:1900-01-01 出版日期:2010-05-20 发布日期:2010-05-20
  • 基金资助:
     

Bioinformatics Analysis of Δ12-Fatty Acid Desaturase in Plants

LIU Wan-Hong;ZHU Li-Qing;YAO Bo   

  1. Department of Biology,Chongqing University of Science and Technology,Chongqing 401331
  • Received:1900-01-01 Revised:1900-01-01 Online:2010-05-20 Published:2010-05-20
  • Supported by:
     

摘要: 运用生物信息学方法,分析不同植物不饱和脂肪酸合成关键酶Δ12-脂肪酸脱氢酶(FAD2)氨基酸序列。结果显示:木本油料植物FAD2属于不稳定蛋白;植物FAD2含有3个极度保守的His-Box;分子进化树揭示木本油料植物关系较近;氨基酸序列不存在转运肽;分子存在多个跨膜结构域,与疏水区域预测结果一致;无规则卷曲是多肽链中的主要结构元件;蛋白保守区域含Delta12-FADS-like结构; FAD2可能受蛋白激酶C磷酸化,位点为Ser140。本研究为开展FAD2蛋白的酶学特性和多不饱和脂肪酸生物合成的分子机理研究提供了重要理论参考。

关键词: &Delta, 12-脂肪酸脱氢酶, 生物信息学, 多不饱和脂肪酸

Abstract: Bioinformatic methods were employed to analyze the amino acid sequences of Δ12-fatty acid desaturase(FAD2), the key synthetase of polyunsaturated fatty acid in different plants. The results were as bellow: FAD2 belongs to a type of unstable protein, containing 3 highly conserved His-Boxes. Phylogenetic tree reveals the close relationship between woody oil plants. There are no transit peptides in amino acid sequence but 4 transmembrane domains, which is consistent with the predictions to hydrophobic domains. Random coils are the major structural elements of polypeptide chain. There are Delta12-FADS-like structures in the conserved domains of SsFAD2. The protein could be phosphorylated by protein kinase C, with the potential phosphorylated site Ser140. This study could privide guidelines to the studies of the enzymatic properties of FAD2 and the mechanisms under the biosynthesis of polyunsaturated fatty acids.

Key words: &Delta, 12-fatty acid desaturase, bioinformatics, polyunsaturated fatty acids

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