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Computational Optimization of Electric Fields for Improving Catalysis of a Designed Kemp Eliminase

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    Research Article

    Computational Optimization of Electric Fields for Improving Catalysis of a Designed Kemp Eliminase
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    † ‡ § ∥ †Kenneth S. Pitzer Center for Theoretical Chemistry, ‡Department of Chemistry, §Department of Chemical and Biomolecular Engineering, and ∥Department of Bioengineering, University of California, Berkeley, Berkeley, California 94720, United States
    ⊥ Chemical Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720, United States
    *E-mail: [email protected]
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    ACS Catalysis

    Cite this: ACS Catal. 2018, 8, 1, 219–227
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    https://doi.org/10.1021/acscatal.7b03151
    Published November 21, 2017
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    Abstract

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    Here we report a computational method to improve efficiency of a de novo designed Kemp eliminase enzyme KE15, by identifying mutations that enhance electric fields and chemical positioning of the substrate that contribute to free energy stabilization of the transition state. Starting from the design that has a kcat/KM of 27 M–1 s–1, the most improved variant introduced four computationally targeted mutations to yield a kcat/KM of 403 M–1 s–1, with almost all of the enzyme improvement realized through a 43-fold improvement in kcat, indicative of a direct impact on the chemical step. This work raises the prospect of computationally designing enzymes that achieve better efficiency with more minimal experimental intervention using electric field optimization as guidance.

    Copyright © 2017 American Chemical Society

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    ACS Catalysis

    Cite this: ACS Catal. 2018, 8, 1, 219–227
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acscatal.7b03151
    Published November 21, 2017
    Copyright © 2017 American Chemical Society
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