Evidence map›Paper›PMID 38831005›Full record

ArticleCommunications chemistry2024

Substrate scope expansion of 4-phenol oxidases by rational enzyme selection and sequence-function relations.

Daniel Eggerichs, Nils Weindorf, Heiner G Weddeling, Inja M Van der Linden, Dirk Tischler

Abstract read
In one paragraph

Article in Communications chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Robots and Minimal, Physics-Informed Features: A Hybrid Framework for Enzyme Catalysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Activity assays for flavoprotein oxidases: an overview.Applied microbiology and biotechnology · 2025
    Review
  6. Chemoenzymatic synthesis.Communications chemistry · 2025
    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.

Daniel EggerichsMicrobial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780, Bochum, Germany.ORCID http://orcid.org/0000-0002-0688-6426
Nils WeindorfMicrobial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780, Bochum, Germany.
Heiner G WeddelingMicrobial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780, Bochum, Germany.ORCID http://orcid.org/0009-0003-2819-1486
Inja M Van der LindenMicrobial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780, Bochum, Germany.
Dirk TischlerMicrobial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780, Bochum, Germany. dirk.tischler@rub.de.ORCID http://orcid.org/0000-0002-6288-2403

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) GRK 2341, 321933041
6 · The paper itself

Abstract

Enzymes are natures' catalysts and will have a lasting impact on (organic) synthesis as they possess unchallenged regio- and stereo selectivity. On the downside, this high selectivity limits enzymes' substrate range and hampers their universal application. Therefore, substrate scope expansion of enzyme families by either modification of known biocatalysts or identification of new members is a key challenge in enzyme-driven catalysis. Here, we present a streamlined approach to rationally select enzymes with proposed functionalities from the ever-increasing amount of available sequence data. In a case study on 4-phenol oxidoreductases, eight enzymes of the oxidase branch were selected from 292 sequences on basis of the properties of first shell residues of the catalytic pocket, guided by the computational tool A

Identifiers

PMID38831005
PMCPMC11148156

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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.