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Updated: May 26, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Rational Enzyme Evolution by Facilitating Correlated Motion along the Reaction
Lianxin Wang1, Yuanfei Xue1, Jia-Ning Wang1
1State Key Laboratory of Precision Spectroscopy, School of Physics and Electronic Science, East China Normal University, Shanghai 200241, China.
Abstract:
Enzymes are highly efficient and specific protein catalysts that play an essential role in regulating metabolic processes in living organisms. By modulating the rates of chemical reactions, enzymes tune fundamental crucial biological functions. Directed evolution is a widely used strategy to enhance protein functionality by selecting variants with desirable traits through random mutation and recombination. However, this approach relies heavily on chemical intuition and demands substantial experimental resources, including labor-intensive mutagenesis. In contrast, rational enzyme engineering leverages mechanistic insights to enhance efficiency and reduce costs. This study presents a mutation strategy guided by the correlated motion of protein during enzymatic reactions, validated through four mutations across two proteins. The results underscore the potential of this physics-based approach to streamline and advance enzyme evolution.
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