Evidence map›Paper›PMID 42297966›Full record

ArticleNature chemical biology2026

Customizing the structure of minimal TIM barrels to craft efficient de novo enzymes.

Julian Beck, Benjamin J Smith, Mark Kriegel, Niayesh Zarifi, Emily Freund, Ahana G Harsha, Jan Hartmann, Roberto A Chica, Birte Höcker

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Stability and cooperativity in chimeric de novo TIM barrels via quarter swapping.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
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.

Julian Beck *Department of Biochemistry, University of Bayreuth, Bayreuth, Germany.
Benjamin J Smith *Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Mark KriegelDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.
Niayesh ZarifiDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.ORCID http://orcid.org/0000-0003-4748-7082
Emily FreundDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.
Ahana G HarshaDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Jan HartmannDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.ORCID http://orcid.org/0009-0008-7160-0034
Roberto A ChicaDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada. rchica@uottawa.ca.ORCID http://orcid.org/0000-0003-3789-9841
Birte HöckerDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany. birte.hoecker@uni-bayreuth.de.ORCID http://orcid.org/0000-0002-8250-9462

Funding

Canada Foundation for Innovation (Fondation canadienne pour l'innovation) 26503EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 951375Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (Conseil de Recherches en Sciences Naturelles et en Génie du Canada) RGPAS-2021-00017Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (Conseil de Recherches en Sciences Naturelles et en Génie du Canada) RGPIN-2021-03484
6 · The paper itself

Abstract

The TIM barrel is the most prevalent fold in natural enzymes, supporting efficient catalysis of diverse reactions. While de novo TIM barrels have been designed, their minimalistic architecture lacks structural elements essential for substrate binding and catalysis. Here, we present CANVAS, a computational workflow that introduces a structural lid into a minimal de novo TIM barrel to anchor catalytic residues and form an active site. Starting from two scaffolds, we designed nine variants with tailored lids for the Kemp elimination. Four showed measurable activity, with the most active reaching a catalytic efficiency of 21,000 M

Identifiers

PMID42297966

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.