Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes

Nicholas J. Weise, Syed T. Ahmed, Fabio Parmeggiani, James L. Galman, Mark S. Dunstan, Simon J. Charnock, David Leys, Nicholas J. Turner

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The suite of biological catalysts found in Nature has the potential to contribute immensely to scientific advancements, ranging from industrial biotechnology to innovations in bioenergy and medical intervention. The endeavour to obtain a catalyst of choice is, however, wrought with challenges. Herein we report the design of a structure-based annotation system for the identification of functionally similar enzymes from diverse sequence backgrounds. Focusing on an enzymatic activity with demonstrated synthetic and therapeutic relevance, five new phenylalanine ammonia lyase (PAL) enzymes were discovered and characterised with respect to their potential applications. The variation and novelty of various desirable traits seen in these previously uncharacterised enzymes demonstrates the importance of effective sequence annotation in unlocking the potential diversity that Nature provides in the search for tailored biological tools. This new method has commercial relevance as a strategy for assaying the 'evolvability' of certain enzyme features, thus streamlining and informing protein engineering efforts.

    Original languageEnglish
    Article number13691
    JournalScientific Reports
    Volume7
    Issue number1
    Early online date20 Oct 2017
    DOIs
    Publication statusPublished - 2017

    Research Beacons, Institutes and Platforms

    • Manchester Institute of Biotechnology

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