Under the induced fit hypothesis, enzyme structure is changed to fit substrate and is recovered to its original form after catalysis occurred, which resembles elastic body motion. We propose novel model to analyze mechanical change of enzyme. This modeling method uses 2 forms of pdb files, apo and holo form of enzyme structure, to analyze the forces by substrate binding. Validation was performed from the data of bacteriophage T4 lysozyme, HIV-1 protease and Candida antarctica lipase B. Elastic body model was applied to select target mutation sites with the aim of activity enhancement. It was discovered that some mutants having change at the forced region showed enhancement of activity in bacteriophage T4 lysozyme. The mutants of Candida antarctica lipase B showed about 4 times enhanced activity when flexible amino acid were introduced in the forced region. And the activity enhancement was due to the increase of kcat value. It inferred that activity enhancement was achieved by flexibility and dynamics increase.
키워드
enzyme flexibilityelastic body modelCandida antarctica lipase B
저자
So Yeon HONG [ Graduate Program of Bioengineering, Seoul National University, Seoul, 151-742. ]
Young Je YOO [ Graduate Program of Bioengineering, School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-742. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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