Earticle

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 can affect the catalytic activity of the enzyme, spring model for enzyme deformation was proposed for the calculation of residual force. And torques at the edges were calculated also.
This new modeling method found that the most twisted region of T4 lysozyme was R80, already known as the hinge-bending region. Thus, this model equation has the validity to guess the enzyme motion. And it was found that the mutations at the edges located far away from R80 increases enzyme activity.
This is the clue that activity enhancement could be achieved by the introduction of hydrophilic residues at some appropriate helix edges in case of hydrolases doing hinge-bending motion during catalysis.

저자

• So Y eon Hong [ Graduate Program in Bioengineering, Seoul National University ]
• Young Je Yoo [ Graduate Program in Bioengineering, Seoul National University ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576