Evidence map›Paper›PMID 41612625›Full record

ArticleAngewandte Chemie (International ed. in English)2026

Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives.

Lilla Gal, Suresh Rohan, Anna Żądło-Dobrowolska, Bianca Hilweg, Judith Müller, Kai Tittmann, Wolfgang Kroutil

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Lilla GalInstitute of Chemistry, University of Graz, Graz, Austria.
Suresh RohanDepartment of Molecular Enzymology, Georg-August University Göttingen, Göttingen, Germany.
Anna Żądło-DobrowolskaInstitute of Chemistry, University of Graz, Graz, Austria.
Bianca HilwegInstitute of Chemistry, University of Graz, Graz, Austria.
Judith MüllerInstitute of Chemistry, University of Graz, Graz, Austria.
Kai TittmannDepartment of Molecular Enzymology, Georg-August University Göttingen, Göttingen, Germany.
Wolfgang KroutilInstitute of Chemistry, University of Graz, Graz, Austria.ORCID 0000-0002-2151-6394

Funding

Erasmus+H2020 Marie Skłodowska-Curie Actions 101073065
6 · The paper itself

Abstract

Although aromatic formylation reactions are highly valuable from a synthetic perspective, a biocatalytic version has not yet been reported. Here, the cofactor-independent multimeric three-component acyltransferase from Chromobacterium sphagni (CsATase) was identified to enable the nonnatural promiscuous regioselective C-formylation of polyphenolic substrates, especially resorcinol derivatives, and thus extending the reaction scope of acyltransferases. Formylation of 4- and 5-substituted resorcinol derivatives gave access to regioselectively mono-formylated products with up to 99% conversion and up to 74% isolated yield. Formylation of phloroglucinol led to the di-formylated product with 99% conversion, outperforming chemical methods. Structural analysis of CsATase by X-ray crystallography provided insights into its active site.

Indexed as

AcyltransferasesResorcinolsBiocatalysisCatalytic DomainCrystallography, X-RayModels, MolecularMolecular StructureStereoisomerismAcyltransferasesresorcinolResorcinolsacyltransferasesbiocatalysisbiocatalytic formylationresorcinol derivativesX‐ray structure elucidation

Identifiers

PMID41612625
PMCPMC12955522

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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.