Predicting an improvement of secondary catalytic activity of promiscuos isochorismate pyruvate lyase by computational design

Sergio Matí, Juan Andrés, Vicent Moliner, Estanislao Silla, Iñaki Tuñón, Juan Bertrán

    Research output: Contribution to journalArticleResearchpeer-review

    23 Citations (Scopus)

    Abstract

    Improvement of the secondary catalytic activity of promiscuous enzymes can be guided by computational protein engineering. This methodology has been applied to isochorismate pyruvate lyase (IPL) that catalyzes isochorismate transformation into pyruvate and salicylate but it also presents secondary activity catalyzing the transformation of chorismate into prephenate. According to the computational results, a mutation of Val by Ile at position 38 would keep the enol pyruvyl moiety of the substrate in a diaxial conformation, closer to the TS geometry, thus reducing the free energy barrier of the chemical reaction 4.4 kcal·mol-1 with respect to the native IPL. Copyright © 2008 American Chemical Society.
    Original languageEnglish
    Pages (from-to)2894-2895
    JournalJournal of the American Chemical Society
    Volume130
    Issue number10
    DOIs
    Publication statusPublished - 12 Mar 2008

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