Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes

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 challeng...

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Autores principales:	Nicholas J. Weise, Syed T. Ahmed, Fabio Parmeggiani, James L. Galman, Mark S. Dunstan, Simon J. Charnock, David Leys, Nicholas J. Turner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7bb9d4a74a89407ab9d72a5cb2e2d579
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spelling	oai:doaj.org-article:7bb9d4a74a89407ab9d72a5cb2e2d5792021-12-02T15:05:41ZZymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes10.1038/s41598-017-13990-02045-2322https://doaj.org/article/7bb9d4a74a89407ab9d72a5cb2e2d5792017-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-13990-0https://doaj.org/toc/2045-2322Abstract 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.Nicholas J. WeiseSyed T. AhmedFabio ParmeggianiJames L. GalmanMark S. DunstanSimon J. CharnockDavid LeysNicholas J. TurnerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nicholas J. Weise Syed T. Ahmed Fabio Parmeggiani James L. Galman Mark S. Dunstan Simon J. Charnock David Leys Nicholas J. Turner Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
description	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.
format	article
author	Nicholas J. Weise Syed T. Ahmed Fabio Parmeggiani James L. Galman Mark S. Dunstan Simon J. Charnock David Leys Nicholas J. Turner
author_facet	Nicholas J. Weise Syed T. Ahmed Fabio Parmeggiani James L. Galman Mark S. Dunstan Simon J. Charnock David Leys Nicholas J. Turner
author_sort	Nicholas J. Weise
title	Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
title_short	Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
title_full	Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
title_fullStr	Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
title_full_unstemmed	Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
title_sort	zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7bb9d4a74a89407ab9d72a5cb2e2d579
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Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes

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