Evidence map›Paper›PMID 31611633›Full record

ArticleNature chemistry2019

A marine viral halogenase that iodinates diverse substrates.

Danai S Gkotsi, Hannes Ludewig, Sunil V Sharma, Jack A Connolly, Jagwinder Dhaliwal, Yunpeng Wang, William P Unsworth, Richard J K Taylor, Matthew M W McLachlan, Stephen Shanahan and 2 more

Abstract read
In one paragraph

Article in Nature chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
9.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 98 citations in OpenAlex.

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  7. Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025
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  8. Sequential Reconstruction of Calicheamicin γAngewandte Chemie (International ed. in English) · 2025
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  18. Biosynthetic mechanism of the yellow pigments in the marine bacteriumApplied and environmental microbiology · 2024
    Article
  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Danai S GkotsiSchool of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
Hannes Ludewig *School of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
Sunil V Sharma *School of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
Jack A ConnollySchool of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
Jagwinder DhaliwalSchool of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
Yunpeng WangSchool of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK.
William P UnsworthDepartment of Chemistry, University of York, Heslington, York, UK.
Richard J K TaylorDepartment of Chemistry, University of York, Heslington, York, UK.
Matthew M W McLachlanSyngenta, Jealott's Hill International Research Centre, Bracknell, Berkshire, UK.
Stephen ShanahanSyngenta, Jealott's Hill International Research Centre, Bracknell, Berkshire, UK.
James H NaismithDivision of Structural Biology, Wellcome Trust Centre of Human Genomics, Oxford, UK.ORCID http://orcid.org/0000-0001-6744-5061
Rebecca J M GossSchool of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife, UK. rjmg@st-andrews.ac.uk.ORCID http://orcid.org/0000-0001-9869-8205
University of St Andrews · GBUniversity of York · GBCentre for Human Genetics · GBSyngenta (United Kingdom) · GBThe University of Queensland · AU

Funding

European Research Council 614779Wellcome Trust
6 · The paper itself

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.

Indexed as

BacteriophagesChemistry Techniques, SyntheticCyanobacteriaHalogenationKineticsMolecular StructureOxidoreductasesSubstrate SpecificityOxidoreductases

Identifiers

PMID31611633
PMCPMC6875430
OpenAlexW2979824003

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.