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Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes

DOI: 10.1038/s41598-017-13990-0 DOI Help

Authors: Nicholas J. Weise (Manchester Institute of Biotechnology, University of Manchester) , Syed T. Ahmed (Manchester Institute of Biotechnology, University of Manchester) , Fabio Parmeggiani (Manchester Institute of Biotechnology, University of Manchester) , James L. Galman (Manchester Institute of Biotechnology, University of Manchester) , Mark S. Dunstan (Manchester Institute of Biotechnology, University of Manchester) , Simon J. Charnock (Prozomix Ltd) , David Leys (Manchester Institute of Biotechnology, University of Manchester) , Nicholas J. Turner (Manchester Institute of Biotechnology, University of Manchester)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Scientific Reports , VOL 7

State: Published (Approved)
Published: October 2017
Diamond Proposal Number(s): 9887

Open Access Open Access

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.

Journal Keywords: Biocatalysis; X-ray crystallography

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Documents:
s41598-017-13990-0.pdf