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Rapid estimation of catalytic efficiency by cumulative atomic multipole moments: application to ketosteroid isomerase mutants

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)945-955
Number of pages11
JournalJournal of Chemical Theory and Computation
Volume13
Issue number2
Early online date19 Jan 2017
DOIs
DateAccepted/In press - 19 Jan 2017
DateE-pub ahead of print - 19 Jan 2017
DatePublished (current) - 14 Feb 2017

Abstract

We propose a simple atomic multipole electrostatic model to rapidly evaluate the effects of mutation on enzyme activity and test its performance on wild-type and mutant ketosteroid isomerase. The predictions of our atomic multipole model are similar to those obtained with symmetry-adapted perturbation theory at a fraction of the computational cost. We further show that this approach is relatively insensitive to the precise amino acid side chain conformation in mutants and may thus be useful in computational enzyme (re)design.

    Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

    Research areas

  • enzyme catalysis, ketosteroid isomerase, cumulative atomic multipole moments, electrostatic catalysis

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at http://pubs.acs.org/doi/abs/10.1021/acs.jctc.6b01131. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 2.54 MB, PDF document

    Licence: CC BY-NC

  • Supplementary information PDF

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at http://pubs.acs.org/doi/abs/10.1021/acs.jctc.6b01131. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 995 KB, PDF document

    Licence: CC BY-NC

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