Evidence map›Paper›PMID 35799064›Full record

ArticleNature chemical biology2022

Functional metagenomic screening identifies an unexpected β-glucuronidase.

Stefanie Neun, Paul Brear, Eleanor Campbell, Theodora Tryfona, Kamel El Omari, Armin Wagner, Paul Dupree, Marko Hyvönen, Florian Hollfelder

Abstract read
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In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Activity-Based Tracking of Glycan Turnover in Microbiomes.Journal of the American Chemical Society · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. The Impact of Metagenomics on Biocatalysis.Angewandte Chemie (International ed. in English) · 2024
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Stefanie NeunDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-2469-6984
Paul BrearDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-4045-0474
Eleanor CampbellDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Theodora TryfonaDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-1618-3521
Kamel El OmariDiamond Light Source, Harwell Science and Innovation Campus, Didcot, UK.ORCID http://orcid.org/0000-0003-3506-6045
Armin WagnerDiamond Light Source, Harwell Science and Innovation Campus, Didcot, UK.ORCID http://orcid.org/0000-0001-8995-7324
Paul DupreeDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-9270-6286
Marko HyvönenDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-8683-4070
Florian HollfelderDepartment of Biochemistry, University of Cambridge, Cambridge, UK. fh111@cam.ac.uk.ORCID http://orcid.org/0000-0002-1367-6312

Funding

Biotechnology and Biological Sciences Research Council BB/T003545/1Biotechnology and Biological Sciences Research Council BB/W000504/1
6 · The paper itself

Abstract

The abundance of recorded protein sequence data stands in contrast to the small number of experimentally verified functional annotation. Here we screened a million-membered metagenomic library at ultrahigh throughput in microfluidic droplets for β-glucuronidase activity. We identified SN243, a genuine β-glucuronidase with little homology to previously studied enzymes of this type, as a glycoside hydrolase 3 family member. This glycoside hydrolase family contains only one recently added β-glucuronidase, showing that a functional metagenomic approach can shed light on assignments that are currently 'unpredictable' by bioinformatics. Kinetic analyses of SN243 characterized it as a promiscuous catalyst and structural analysis suggests regions of divergence from homologous glycoside hydrolase 3 members creating a wide-open active site. With a screening throughput of >10

Indexed as

GlucuronidaseMetagenomicsGene LibraryGlycoside HydrolasesMetagenomeGlucuronidaseGlycoside Hydrolases

Identifiers

What OpenQuestion holds

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Registered trials

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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.