Complementary Experimental and Theoretical Analysis of Subtilisin Binding and Catalysis

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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.***