Evidence map›Paper›PMID 35046426›Full record

ArticleNature communications2022

Merging enzymes with chemocatalysis for amide bond synthesis.

Luis Bering, Elliott J Craven, Stanley A Sowerby Thomas, Sarah A Shepherd, Jason Micklefield

Abstract read
In one paragraph

Article in Nature communications, 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. Review
  4. A tailored CoA ligase-Nature catalysis · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Enzymatic Cascades for Stereoselective and Regioselective Amide Bond Assembly.Angewandte Chemie (International ed. in English) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Chemical Constituents of the MushroomMolecules (Basel, Switzerland) · 2023
    Article
  18. Article
  19. Combined chemoenzymatic strategy for sustainable continuous synthesis of the natural product hordenine.Green chemistry : an international journal and green chemistry resource : GC · 2022
    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

5 authors.

Luis BeringDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Elliott J CravenDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Stanley A Sowerby ThomasDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Sarah A ShepherdDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.ORCID http://orcid.org/0000-0002-7321-1234
Jason MicklefieldDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. jason.micklefield@manchester.ac.uk.ORCID http://orcid.org/0000-0001-8951-4873

Funding

Biotechnology and Biological Sciences Research Council BB/R01034X/1
6 · The paper itself

Abstract

Amides are one of the most fundamental chemical bonds in nature. In addition to proteins and other metabolites, many valuable synthetic products comprise amide bonds. Despite this, there is a need for more sustainable amide synthesis. Herein, we report an integrated next generation multi-catalytic system, merging nitrile hydratase enzymes with a Cu-catalysed N-arylation reaction in a single reaction vessel, for the construction of ubiquitous amide bonds. This synergistic one-pot combination of chemo- and biocatalysis provides an amide bond disconnection to precursors, that are orthogonal to those in classical amide synthesis, obviating the need for protecting groups and delivering amides in a manner unachievable using existing catalytic regimes. Our integrated approach also affords broad scope, very high (molar) substrate loading, and has excellent functional group tolerance, telescoping routes to natural product derivatives, drug molecules, and challenging chiral amides under environmentally friendly conditions at scale.

Indexed as

BiocatalysisAmidesEnzymesKineticsNitrilesStereoisomerismAmidesEnzymesNitriles

Identifiers

PMID35046426
PMCPMC8770729

What OpenQuestion holds

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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.