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Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology

Non-heme iron-dependent oxygenases catalyse the incorporation of O(2) into a wide range of biological molecules and use diverse strategies to activate their substrates. Recent kinetic studies, including in crystallo, have provided experimental support for some of the intermediates used by different...

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Detalles Bibliográficos
Autores principales: White, Mark D, Flashman, Emily
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879150/
https://www.ncbi.nlm.nih.gov/pubmed/27015291
http://dx.doi.org/10.1016/j.cbpa.2016.02.017
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author White, Mark D
Flashman, Emily
author_facet White, Mark D
Flashman, Emily
author_sort White, Mark D
collection PubMed
description Non-heme iron-dependent oxygenases catalyse the incorporation of O(2) into a wide range of biological molecules and use diverse strategies to activate their substrates. Recent kinetic studies, including in crystallo, have provided experimental support for some of the intermediates used by different subclasses of this enzyme family. Plant non-heme iron-dependent oxygenases have diverse and important biological roles, including in growth signalling, stress responses and secondary metabolism. Recently identified roles include in strigolactone biosynthesis, O-demethylation in morphine biosynthesis and regulating the stability of hypoxia-responsive transcription factors. We discuss current structural and mechanistic understanding of plant non-heme iron oxygenases, and how their chemical/genetic manipulation could have agricultural benefit, for example, for improved yield, stress tolerance or herbicide development.
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spelling pubmed-48791502016-06-02 Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology White, Mark D Flashman, Emily Curr Opin Chem Biol Article Non-heme iron-dependent oxygenases catalyse the incorporation of O(2) into a wide range of biological molecules and use diverse strategies to activate their substrates. Recent kinetic studies, including in crystallo, have provided experimental support for some of the intermediates used by different subclasses of this enzyme family. Plant non-heme iron-dependent oxygenases have diverse and important biological roles, including in growth signalling, stress responses and secondary metabolism. Recently identified roles include in strigolactone biosynthesis, O-demethylation in morphine biosynthesis and regulating the stability of hypoxia-responsive transcription factors. We discuss current structural and mechanistic understanding of plant non-heme iron oxygenases, and how their chemical/genetic manipulation could have agricultural benefit, for example, for improved yield, stress tolerance or herbicide development. Elsevier 2016-04 /pmc/articles/PMC4879150/ /pubmed/27015291 http://dx.doi.org/10.1016/j.cbpa.2016.02.017 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
White, Mark D
Flashman, Emily
Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title_full Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title_fullStr Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title_full_unstemmed Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title_short Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
title_sort catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879150/
https://www.ncbi.nlm.nih.gov/pubmed/27015291
http://dx.doi.org/10.1016/j.cbpa.2016.02.017
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