| 负电荷区Glu224-Glu225-Asp226对精氨酸激酶结构和功能的影响 |
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| 引用本文： | 潘云帆,汪劲松.负电荷区Glu224-Glu225-Asp226对精氨酸激酶结构和功能的影响[J].辽宁化工,2012,41(7):643-644,646. |
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| 作者姓名： | 潘云帆 汪劲松 |
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| 作者单位： | 1. 中国地质大学环境学院,湖北武汉,430074
2. 湖北师范学院生命科学学院,湖北黄石,435002 |
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| 基金项目： | 湖北省自然科学基金(No:2005AB192);黄石市二0一0年度科技计划项目资助 |
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| 摘 要： | 精氨酸激酶224-226氨基酸残基是高度保守的负电荷区域,其在激酶家族的地位一直是学术界关注的问题之一.将刀额新对虾精氨酸激酶高度保守的负电荷密集区氨基酸残基Glu224-Glu225-Asp226突变为Gly224-Gly225-Gly226,消除负电荷性质.突变体在Rosetta中实现了可溶性表达,用His-tag亲和层析纯化了蛋白.采用酶括力测定及光谱学分析等手段的研究结果表明,该“负电荷区”对酶的结构与功能有着重要的影响.
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| 关 键 词： | 精氨酸激酶 负电荷密集区 Glu224-Glu225-Asp226 结构和功能 |
Study on the Role of Glu224-Glu225-Asp226 in the Construction and Function of Arginine Kinase |
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| PAN Yun-fan
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WANG Jin-song.Study on the Role of Glu224-Glu225-Asp226 in the Construction and Function of Arginine Kinase[J].Liaoning Chemical Industry,2012,41(7):643-644,646. |
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| Authors: | PAN Yun-fan WANG Jin-song |
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| Affiliation: | 1.School of Environmental Studies,China University of Geosciences,Hubei Wuhan 430074,China; 2.College of Life Science,Hubei Normal University,Hubei Huangshi 435002,China) |
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| Abstract: | With the help of site-directed mutagenesis on certain highly conservative amino acid residues Glu224-Glu225-Asp226 to Gly224-Gly225-Gly226 and the method of spectroscopy,the difference between mutant and wild-type arginine kinase on the affinity to substrate was compared;the catalytic activity to analyze the role of such amino acid residues in the enzyme was contrasted,in order to study the effect of negative charge intensive areas on the protein conformational stability. |
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| Keywords: | arginine kinase intensive areas of negative charge Glu224-Glu225-Asp226 structure and function |
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