원문정보
초록
영어
Enzyme activity is an important character because industry requires efficient catalysts. In
this study, bacteriophage T4 lysozyme was selected as a model enzyme and the flexibility
of the mutants was analyzed to understand the mechanism of activity enhancement. The
group having enhanced activity showed a tendency that the changed residues in the
mutants were, in many cases, Glu, Asp and many of them were located in the helix edge.
Because the flexibility is related with the enzyme motion and this flexibility factor can
affect the catalytic activity of the enzyme, spring model for enzyme deformation was
proposed as the tool of target sites selection in this work. The residues having the highest
rigidity value were located in the helix edges and this shows the possibility of the
selection of enzyme residues for activity enhancement using only B-factor and the Root
Mean Square Deviation (RMSD) between the Cα co-ordinates of the free-form and the
substrate bound form of enzyme.