A marine viral halogenase that iodinates diverse substrates
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.
Citation
Gkotsi , D S , Ludewig , H , Sharma , S V , Connolly , J A , Dhaliwal , J , Wang , Y , Unsworth , W P , Taylor , R J K , McLachlan , M M W , Shanahan , S , Naismith , J H & Goss , R J M 2019 , ' A marine viral halogenase that iodinates diverse substrates ' , Nature Chemistry , vol. 11 , no. 12 , pp. 1091–1097 . https://doi.org/10.1038/s41557-019-0349-z
Publication
Nature Chemistry
Status
Peer reviewed
ISSN
1755-4349Type
Journal article
Rights
Copyright © The Author(s), under exclusive licence to Springer Nature Limited 2019. This work has been made available online in accordance with publisher policies or with permission. Permission for further reuse of this content should be sought from the publisher or the rights holder. This is the author created accepted manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.1038/s41557-019-0349-z
Description
We thank the European Research Council under the European Union’s Seventh Framework Programme (FP7/2007–2013/ERC grant agreement no. 614779 GenoChemetics to R.J.M.G.), Syngenta and Wellcome ISSF (grant no. 204821/Z/16/Z to D.S.G.) for generous financial support.Collections
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