The Relationship between Physical Property and Function of Highly Activated Mutants of Thermolysin

摘要

Thermolysin mutants having a variety of amino acid at the 119th position arc designed by considering electrostatic field effect upon the active area. The most activated mutant has five times higher hydrolytic activity than the wild type. Negative correlation between the activity and the thermal stability is observed. A combined effect of the flexibility of the substrate binding site and the negative electrostatic field around the site is suggested as a key to enhance the activity.