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Updated: Jul 10, 2026
09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Structure and dynamics of a molten globular enzyme
Konstantin Pervushin1, Katherina Vamvaca, Beat Vögeli
1Laboratory of Physical Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
Nature Structural & Molecular Biology
|November 13, 2007
Summary
Engineered enzymes can be highly active despite structural disorder. This study shows a flexible enzyme uses an induced-fit mechanism for efficient catalysis, challenging previous assumptions about protein dynamics and enzyme efficiency.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Protein dynamics are increasingly recognized for their role in enzyme catalysis.
- Structural disorder in proteins is traditionally thought to decrease catalytic efficiency.
- An engineered chorismate mutase exhibiting molten globule properties challenges this notion.
Purpose of the Study:
- To investigate the structural and dynamic properties of an engineered chorismate mutase in complex with a transition-state analog.
- To elucidate the relationship between protein flexibility and catalytic efficiency in this enzyme.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy to characterize the enzyme-ligand complex.
- Pre-steady-state kinetic analysis to study the binding mechanism.
Main Results:
- The enzyme-ligand complex adopts a designed helix-bundle structure.
- Significant protein flexibility on the millisecond timescale was observed throughout the enzyme.
- Ligand binding proceeds via an induced-fit mechanism occurring on the same timescale as catalysis.
Conclusions:
- Global conformational plasticity is linked to efficient enzyme catalysis.
- The findings challenge the conventional view that structural disorder limits catalytic efficiency.
- This engineered enzyme provides a model for understanding the role of dynamics in enzyme function.
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