| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 69539 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 5 Pages |
•The mutations in activity-enhanced mutants of bacteriophage T4 lysozyme were investigated to be almost changed to Glu or Asp.•The mutation sites were investigated to be located at the helix edges.•The flexibility of mutated sites was analyzed to be increased in most cases.
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
