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Updated: Mar 17, 2026
09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
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DMSO enhanced conformational switch of an interfacial enzyme
Richard J Lindsay1,2, Quentin R Johnson2,3, Wilfredo Evangelista2,4
1UT-ORNL Graduate School of Genome Science and Technology, Knoxville, TN, 37996.
Biopolymers
|July 28, 2016
Summary
Dimethyl sulfoxide (DMSO) enhances lipase activity by altering its structure. Molecular dynamics simulations show DMSO shifts lipase conformation to an open state, increasing enzyme function.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Interfacial proteins, like microbial lipase, operate in complex environments.
- Lipase activation in oil-water emulsions is crucial for enzymatic functions.
- Dimethyl sulfoxide (DMSO) is known to increase lipase activity, but the mechanism is unclear.
Purpose of the Study:
- To investigate the mechanism by which DMSO enhances lipase activity.
- To analyze the effect of DMSO on the gating mechanism dynamics of lipase.
- To understand the role of the α5 region in lipase gating and activation.
Main Methods:
- All-atom molecular dynamics simulations were employed.
- Lipase behavior in binary solutions (water-DMSO) was simulated.
- Conformational analysis focused on the lipase's α5 region and gorge structure.
Main Results:
- DMSO shifts lipase conformation from a closed-gorge to an open-gorge state.
- Increased DMSO concentrations (45% and 60%) widen the enzyme's access channel.
- The α5 region becomes more α-helical with increasing DMSO, correlating with activation.
Conclusions:
- The structural ordering of the α5 region is essential for lipase gating.
- DMSO-induced structural changes in the α5 region are key to enhanced lipase activity.
- This study elucidates the molecular mechanism behind DMSO's effect on lipase.
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