Evidence map›Paper›PMID 38438341›Full record

ArticleNature communications2024

A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme.

Amy E Hutton, Jake Foster, Rebecca Crawshaw, Florence J Hardy, Linus O Johannissen, Thomas M Lister, Emilie F Gérard, Zachary Birch-Price, Richard Obexer, Sam Hay and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

11 authors.

Amy E HuttonManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Jake FosterManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Rebecca CrawshawManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Florence J HardyManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0003-0671-0209
Linus O JohannissenManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0002-0916-9094
Thomas M ListerManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Emilie F GérardManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Zachary Birch-PriceManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.
Richard ObexerManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0002-4940-3543
Sam HayManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0003-3274-0938
Anthony P GreenManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK. Anthony.green@manchester.ac.uk.ORCID 0000-0003-0454-1798

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M017702/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M027023/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S507040/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S507969/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/W014483/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X000974/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X010724/1
6 · The paper itself

Abstract

Directed evolution of computationally designed enzymes has provided new insights into the emergence of sophisticated catalytic sites in proteins. In this regard, we have recently shown that a histidine nucleophile and a flexible arginine can work in synergy to accelerate the Morita-Baylis-Hillman (MBH) reaction with unrivalled efficiency. Here, we show that replacing the catalytic histidine with a non-canonical N

Indexed as

ArginineHistidineBiological EvolutionCatalysisEngineeringMethylhistidinesArginineHistidineMethylhistidines

Identifiers

PMID38438341
PMCPMC10912507

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.