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A Marine Viral Halogenase that Iodinates Diverse Substrates
Oceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet, and therefore, important to life. These organisms are infected by viruses called cyanophages, recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabol...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6875430/ https://www.ncbi.nlm.nih.gov/pubmed/31611633 http://dx.doi.org/10.1038/s41557-019-0349-z |
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author | Gkotsi, Danai S. Ludewig, Hannes Sharma, Sunil V. Connolly, Jack A. Dhaliwal, Jagwinder Wang, Yunpeng Unsworth, William P. Taylor, Richard J. K. McLachlan, Matthew M. W. Shanahan, Stephen Naismith, James H. Goss, Rebecca J. M. |
author_facet | Gkotsi, Danai S. Ludewig, Hannes Sharma, Sunil V. Connolly, Jack A. Dhaliwal, Jagwinder Wang, Yunpeng Unsworth, William P. Taylor, Richard J. K. McLachlan, Matthew M. W. Shanahan, Stephen Naismith, James H. Goss, Rebecca J. M. |
author_sort | Gkotsi, Danai S. |
collection | PubMed |
description | Oceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet, and therefore, important to life. These organisms are infected by viruses called cyanophages, recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabolism. Herein, we report the characterisation of a wild type flavin-dependent viral halogenase (VirX1) from a cyanophage. Notably, halogenases have been previously associated with secondary metabolism, tailoring natural products. Exploration of this viral halogenase reveals it capable of regioselective halogenation of a diverse range of substrates, with a preference for forming aryl iodide species; this has potential implications for the metabolism of the infected host. Until recently, a flavin-dependent halogenase (FDH) capable of iodination in vitro had not been reported. VirX1 is interesting from a biocatalytic perspective showing strikingly broad substrate flexibility, and a clear preference for iodination, as illustrated by kinetic analysis. These factors together render it an attractive tool for synthesis. |
format | Online Article Text |
id | pubmed-6875430 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
spelling | pubmed-68754302020-04-14 A Marine Viral Halogenase that Iodinates Diverse Substrates Gkotsi, Danai S. Ludewig, Hannes Sharma, Sunil V. Connolly, Jack A. Dhaliwal, Jagwinder Wang, Yunpeng Unsworth, William P. Taylor, Richard J. K. McLachlan, Matthew M. W. Shanahan, Stephen Naismith, James H. Goss, Rebecca J. M. Nat Chem Article Oceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet, and therefore, important to life. These organisms are infected by viruses called cyanophages, recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabolism. Herein, we report the characterisation of a wild type flavin-dependent viral halogenase (VirX1) from a cyanophage. Notably, halogenases have been previously associated with secondary metabolism, tailoring natural products. Exploration of this viral halogenase reveals it capable of regioselective halogenation of a diverse range of substrates, with a preference for forming aryl iodide species; this has potential implications for the metabolism of the infected host. Until recently, a flavin-dependent halogenase (FDH) capable of iodination in vitro had not been reported. VirX1 is interesting from a biocatalytic perspective showing strikingly broad substrate flexibility, and a clear preference for iodination, as illustrated by kinetic analysis. These factors together render it an attractive tool for synthesis. 2019-10-14 2019-12 /pmc/articles/PMC6875430/ /pubmed/31611633 http://dx.doi.org/10.1038/s41557-019-0349-z Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Gkotsi, Danai S. Ludewig, Hannes Sharma, Sunil V. Connolly, Jack A. Dhaliwal, Jagwinder Wang, Yunpeng Unsworth, William P. Taylor, Richard J. K. McLachlan, Matthew M. W. Shanahan, Stephen Naismith, James H. Goss, Rebecca J. M. A Marine Viral Halogenase that Iodinates Diverse Substrates |
title | A Marine Viral Halogenase that Iodinates Diverse Substrates |
title_full | A Marine Viral Halogenase that Iodinates Diverse Substrates |
title_fullStr | A Marine Viral Halogenase that Iodinates Diverse Substrates |
title_full_unstemmed | A Marine Viral Halogenase that Iodinates Diverse Substrates |
title_short | A Marine Viral Halogenase that Iodinates Diverse Substrates |
title_sort | marine viral halogenase that iodinates diverse substrates |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6875430/ https://www.ncbi.nlm.nih.gov/pubmed/31611633 http://dx.doi.org/10.1038/s41557-019-0349-z |
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