Gkotsi, Danai S, Ludewig, Hannes, Sharma, Sunil V et al. (9 more authors) (2019) A marine viral halogenase that iodinates diverse substrates. Nature Chemistry. 1091–1097. ISSN 1755-4349
Abstract
Oceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet and are therefore important to life. These organisms are infected by viruses called cyanophages, which have recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabolism. Herein we report the characterization 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 that is capable of iodination in vitro had not been reported. VirX1 is interesting from a biocatalytic perspective as it shows 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 23 Oct 2019 08:30 |
Last Modified: | 16 Oct 2024 16:09 |
Published Version: | https://doi.org/10.1038/s41557-019-0349-z |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1038/s41557-019-0349-z |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:152554 |
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