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Understanding the Entropic Effect in Chorismate Mutase Reaction Catalyzed by Isochorismate-Pyruvate Lyase from Pseudomonas Aeruginosa (PchB)

Abstract

Elucidation the role of entropy in enzymatic reaction can be utilized in de novo design enzymes or protein engineering. Recently, the entropic change in enzyme-catalyzed chorismate mutase reaction brings a doubt by experiment for PchB, that the measured entropic change was comparable to the reported value of uncatalyzed reaction in aqueous solution, which was contrast to the general proposed entropy driven mechanism. Based on the sufficient sampling from quantum mechanics / molecular mechanics molecular dynamics simulations, the entropic effect for PchB-catalyzed chorismate mutase reaction is evaluated for the first time. The calculations suggest, indeed, the PchB-catalyzed chorismate mutase reaction is entropy-driven. The additional entropic penalty is uncovered from the substrate preorganization process, leading to a remarkable apparent entropic effect in reaction. Our findings provide an explanation for the doubt of its large measured entropic effect in experiment and confirm the entropy-driven character of PchB-catalyzed chorismate mutase reaction. The clarified entropy change in enzymatic reaction would provide useful clues for future enzyme design projects.

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Publication details

The article was received on 13 Oct 2018, accepted on 05 Dec 2018 and first published on 06 Dec 2018


Article type: Paper
DOI: 10.1039/C8CY02123F
Citation: Catal. Sci. Technol., 2019, Accepted Manuscript
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    Understanding the Entropic Effect in Chorismate Mutase Reaction Catalyzed by Isochorismate-Pyruvate Lyase from Pseudomonas Aeruginosa (PchB)

    L. Xie, M. Yang and Z. Chen, Catal. Sci. Technol., 2019, Accepted Manuscript , DOI: 10.1039/C8CY02123F

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