원문정보
초록
영어
Activity is an important character of enzyme because industry requires efficient catalysts. In this study, bacteriophage T4 lysozyme was selected as a model enzyme and the flexibility of mutants was analyzed to understand mechanism of activity enhancement. Mutants data were selected in Mutant database and mutants having activity data were chosen. The group having enhanced activity showed a tendency in residue; the changed residues were 7 Glu, 3 Asp, and 1
Pro and 6 of them were located in helix edge. The charge-charge interaction was negligible between the mutated residues and substrate from the point on the distance. The flexibility is related with the enzyme motion and this factor can affect the catalytic activity of the enzyme. The standardized B-factor of Cα can be a measure of residual flexibility. Compared with the wild type, the standardized B-factor change of mutation site in edge region showed a positive
value whilst in helix, a negative value. The mutants having increased activity had more rigid helix body and more flexible helix edge than the wild type. This can be a clue to obtain mutant having enhanced activity.