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钝顶螺旋藻Fe-SOD的结构与进化

Structure and evolvement of Spirulina platensis Fe-SOD

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【作者】 卢敏秦桂香龚兴国郭建军钟文涛

【Author】 LU Min, QIN Gui-xiang, GONG Xing-guo, GUO Jian-jun, ZHONG Wen-tao (Institute of Bio-macromolecule and Enzymatic Engineering ,Zhejiang University, Hangzhou 310027, China)

【机构】 浙江大学生物大分子与酶工程研究所浙江大学生物大分子与酶工程研究所 浙江杭州310027浙江杭州310027浙江杭州310027

【摘要】 超氧化物歧化酶(Superoxide dismutase,SOD)是一类重要的具有抗氧化损伤功能的金属酶.利用生物信息学手段,分析了钝顶螺旋藻(Spirulina platensis)Fe-SOD的结构与进化,结合此蛋白的功能,揭示了两者的内在联系:在结构上,此蛋白的中间区域(26AA~160AA)结构紧凑,为酶的活性中心,两端区域离活性中心较远;在进化上,此蛋白两端区域较中间区域更倾向于发生突变.并且通过Fe-SOD,首次对以上三者间特殊关系的形成机制进行了猜想与假设.

【Abstract】 The Superoxide dismutase (SOD) is a kind of important metal enzyme for protecting organism from toxic oxidation. In this paper, the structure and evolvement of Spirulina platensis Fe-SOD were predicted by the method of bioinformatics. Related to its function, it was showed that: about its structure, the midst of the protein sequence (26AA~160AA) was tight and it was the active center of the enzyme, the ends were far from the active center; as to its evolvement, the ends of the protein sequence were more inclined to mutant. According to the Fe-SOD, a hypothesis about the mechanism of this relation was put forward for the first time.

【基金】 国家技术创新基金资助项目(03C26213300586).
  • 【文献出处】 浙江大学学报(理学版) ,Journal of Zhejiang University(Sciences Edition) , 编辑部邮箱 ,2005年04期
  • 【分类号】Q946.5
  • 【被引频次】2
  • 【下载频次】194
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