Evidence map›Paper›PMID 39944761›Full record

ArticleACS catalysis2025

Evolutionary Specialization of a Promiscuous Designer Enzyme.

Reuben B Leveson-Gower, Laura Tiessler-Sala, Henriette J Rozeboom, Andy-Mark W H Thunnissen, Jean-Didier Maréchal, Gerard Roelfes

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026
    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

6 authors.

Reuben B Leveson-GowerStratingh Institute for Chemistry, University of Groningen, 9747AG Groningen, The Netherlands.
Laura Tiessler-SalaInsilichem, Departament de Química, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès, Spain.
Henriette J RozeboomGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.
Andy-Mark W H ThunnissenGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.ORCID https://orcid.org/0000-0002-1915-9850
Jean-Didier MaréchalInsilichem, Departament de Química, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès, Spain.ORCID https://orcid.org/0000-0002-8344-9043
Gerard RoelfesStratingh Institute for Chemistry, University of Groningen, 9747AG Groningen, The Netherlands.ORCID https://orcid.org/0000-0002-0364-9564

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolution of a promiscuous enzyme for its various activities often results in catalytically specialized variants. This is an important natural mechanism to ensure the proper functioning of natural metabolic networks. It also acts as both a curse and blessing for enzyme engineers, where enzymes that have undergone directed evolution may exhibit exquisite selectivity at the expense of a diminished overall catalytic repertoire. We previously performed two independent directed evolution campaigns on a promiscuous designer enzyme that leverages the unique properties of a noncanonical amino acid (ncAA)

Identifiers

PMID39944761
PMCPMC11811923

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.