A marine viral halogenase that iodinates diverse substrates

TY - JOUR

T1 - A marine viral halogenase that iodinates diverse substrates

AU - Gkotsi, Danai S

AU - Ludewig, Hannes

AU - Sharma, Sunil V

AU - Connolly, Jack A

AU - Dhaliwal, Jagwinder

AU - Wang, Yunpeng

AU - Unsworth, William P

AU - Taylor, Richard J K

AU - McLachlan, Matthew M W

AU - Shanahan, Stephen

AU - Naismith, James H

AU - Goss, Rebecca J M

N1 - 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.

PY - 2019/12/1

Y1 - 2019/12/1

N2 - 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.

AB - 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.

U2 - 10.1038/s41557-019-0349-z

DO - 10.1038/s41557-019-0349-z

M3 - Article

C2 - 31611633

SN - 1755-4330

VL - 11

SP - 1091

EP - 1097

JO - Nature Chemistry

JF - Nature Chemistry

IS - 12

ER -