期刊
CHEMICAL PHYSICS LETTERS
卷 507, 期 1-3, 页码 157-161出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cplett.2011.03.046
关键词
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资金
- Japan Society for the Promotion of Science (JSPS) [22 685 003, 20 750 004]
- Theoretical and Computational Biophysics group at the Beckman Institute, University of Illinois at Urbana-Champaign
- Grants-in-Aid for Scientific Research [23656533, 22360350, 22685003, 22657031, 22121519, 22370061] Funding Source: KAKEN
In order to understand roles of E168 and Y170 residues in loop-segment (N166-V177) of nylon-6 byproduct-degrading enzymes, we determined substrate-binding structures of E168Q and Y170F mutants using molecular dynamics simulation with in silico mutations. We found that movement of the loop-segment plays key roles not only in allowing the substrate to be bound by induced fit mechanism but also in forming water-exclusive environment. Fluctuations of the loop-segment in the mutant enzymes caused a room near the catalytic site, where water molecules can access. We propose that the water located exclusivity at the catalytic site is a major factor of its activity. (C) 2011 Elsevier B.V. All rights reserved.
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