Chemoenzymatic Route toward a De Novo Enantioselective Total Synthesis of (S)-Baclofen Based on Metal-Catalyzed Hydroformylation and Enzymatic Transamination.

Feodor Belov, Hannah Bork, Luise Hänel, Manideep V Kollipara, Matthias Höhne, Harald Gröger, Jan von Langermann

Abstract read

In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. 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.

Feodor BelovInstitute of Chemistry, Biocatalytic Synthesis Group, Otto von Guericke University of Magdeburg, Building 28, Universitätsplatz 2, 39106, Magdeburg, Germany.

Hannah BorkFaculty of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615, Bielefeld, Germany.

Luise HänelInstitute of Biochemistry, Protein Biochemistry Group, University of Greifswald, Felix-Hausdorff-Str. 4, 17489, Greifswald, Germany.

Manideep V KolliparaInstitute of Biochemistry, Protein Biochemistry Group, University of Greifswald, Felix-Hausdorff-Str. 4, 17489, Greifswald, Germany.

Matthias HöhneInstitute of Chemistry, Biocatalysis Group, Technical University of Berlin, Müller-Breslau-Strasse 10, 10623, Berlin, Germany.ORCID https://orcid.org/0000-0002-2542-725X

Harald GrögerFaculty of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615, Bielefeld, Germany.ORCID https://orcid.org/0000-0001-8582-2107

Jan von LangermannInstitute of Chemistry, Biocatalytic Synthesis Group, Otto von Guericke University of Magdeburg, Building 28, Universitätsplatz 2, 39106, Magdeburg, Germany.ORCID https://orcid.org/0000-0001-9302-9803

Funding

Bundesministerium für Wirtschaft und Klimaschutz ZF4402103CR9Bundesministerium für Wirtschaft und Klimaschutz ZF4832701CR9Bundesministerium für Wirtschaft und Klimaschutz ZF4842701CR9Deutsche Forschungsgemeinschaft 450014604

6 · The paper itself

Abstract

This study explores the chemoenzymatic synthesis of (S)-baclofen, which involves a sequential combination of transition metal catalysis and biocatalysis. The synthesis approach starts from a readily accessible cinnamic acid ester that is converted using a rhodium-based hydroformylation catalyst toward the corresponding chiral aldehyde. This compound is subsequently converted via a transaminase-catalyzed reaction system that yields the desired β-chiral amino acid ester and the final free β-chiral amino acid (S)-baclofen after a simple hydrolysis reaction. This synthesis concept does provide high atom efficiency and does not require an additional chiral resolution step of a racemic product.

Indexed as

BaclofenRhodiumTransaminasesAminationBiocatalysisCatalysisCinnamatesMolecular StructureStereoisomerismBaclofenCinnamatescinnamic acidRhodiumTransaminasesaminesbiocatalysiscascadechiralhomogeneous catalysis

Identifiers

PMID40504839

DOI10.1002/cbic.202500108

PMCPMC12376269

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

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.