Complementary Experimental and Theoretical Analysis of Subtilisin Binding and Catalysis

研究枯草菌素酶是为了了解酶结合和催化的本质，这是一个对生物学和化学都很重要的领域。这种酶是这种研究的理想系统，因为已知x射线结构具有高分辨率，更重要的是，许多突变变体的晶体结构已经和正在解决。作用机制明确，并分别分析了一级结构变化对结合和催化的影响。其他酶也被研究过位点特异性诱变，但没有一种酶能像枯草杆菌素那样，同时具有优异而丰富的晶体结构和多种结合和催化突变变体。应该实现对丝氨酸蛋白酶催化细节的新见解。这也将促进理论方法的发展和完善，以研究许多其他大分子分子以及酶的结合和催化作用

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.***