Abstract
Abstract Enzymes are essential biological molecules and widely used in industry. Therefore, investigating the mechanisms underlying how enzyme activity is changed by mutations may have widespread clinical and industrial applications as well as understanding of enzyme catalysis. In this paper, various reported mutants of bacteriophage T4 lysozyme were analyzed to investigate the relationship between enzyme activity and flexibility. The activity-enhanced mutants of bacteriophage T4 lysozyme demonstrated a tendency for mutations to localize to the edge of helices and to involve substitutions to flexible amino acids such as glutamic acid and aspartic acid. Additionally, the mutated residues were shown to demonstrate increased flexibility in B-factor. These findings suggest that flexibility modulation may be a feasible means to enhance enzyme activity.
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