Complementary Experimental and Theoretical Analysis of Subtilisin Binding and Catalysis

枯草杆菌蛋白酶结合和催化的补充实验和理论分析

• 批准号: 8714775
• 负责人: Peter Kollman
• 金额: --
• 依托单位: University of California-San Francisco
• 依托单位国家: 美国
• 项目类别: Continuing grant
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-04-15 至 1991-09-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8714775&HistoricalAwards=false
• 关键词: Complementary; Experimental; Theoretical; Analysis; Subtilisin

The enzyme subtilisin will be studied in order to understand the nature of enzyme binding and catalysis, an area of importance both to biology and chemistry. This enzyme is an ideal system for such a study because the x-ray structure is known to high resolution and, more importantly, many crystal structures of mutant variants have been and are being solved. The mechanism of action is clear and the effects of changes in the primary structures on both binding and catalysis have been analyzed separately. Other enzymes have been studied with site specific mutagenesis, but none have the combination of excellent and abundant crystal structures and this wide variety of binding and catalytic mutant variants that subtilisin does. New insights into the details of serine protease catalysis should be realized. This should also catalyze the development and refinement of theoretical methods for studying binding and catalysis in many other macromolecular molecules as well as in enzymes.***

将对枯草杆菌蛋白酶进行研究， 酶结合和催化的性质， 对生物学和化学都很重要。 这种酶是一种 这是一个理想的系统，因为X射线结构是 已知高分辨率，更重要是，许多晶体 突变变体的结构已经并且正在被解决。 作用机制明确，影响变化 在结合和催化的一级结构中， 分别进行了分析。 其他的酶也被研究过 但没有一个能结合 具有优良和丰富的晶体结构， 枯草杆菌蛋白酶的多种结合和催化突变变体 可以这 丝氨酸蛋白酶催化细节的新见解 应该实现。 这也将促进 发展和完善的理论方法， 研究许多其他大分子中的结合和催化作用 分子以及酶中的。