Evidence map›Paper›PMID 41085469›Full record

ArticleJournal of the American Chemical Society2025

Mechanistic Elucidation and Stereochemical Consequences of Alternative Binding of Alkenyl Substrates by Engineered Arylmalonate Decarboxylase.

Elske van der Pol, Thomas Schlatzer, Gyula Hoffka, Bruno Di Geronimo, Johannes Eder, Anna K Schweiger, Marianna Karava, Dominik Gross, Roland C Fischer, Daniel Kracher and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 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. 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

15 authors.

Elske van der PolInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.
Thomas SchlatzerInstitute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria.ORCID 0000-0001-5034-0968
Gyula HoffkaDepartment of Chemistry, Lund University, Box 124, 221 00 Lund, Sweden.
Bruno Di GeronimoSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, Georgia 30318, United States.ORCID 0000-0003-1822-7142
Johannes EderInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.ORCID 0009-0002-8408-2279
Anna K SchweigerInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.
Marianna KaravaInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.
Dominik GrossInstitute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria.ORCID 0009-0004-5025-0961
Roland C FischerInstitute for Inorganic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria.ORCID 0000-0001-9523-5010
Daniel KracherInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.ORCID 0000-0002-3856-3170
Romas KazlauskasDepartment of Biochemistry, Molecular Biology and Biophysics, and The Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, Minnesota 55108, United States.
Kenji MiyamotoDepartment of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.ORCID 0000-0003-0080-4693
Shina Caroline Lynn KamerlinDepartment of Chemistry, Lund University, Box 124, 221 00 Lund, Sweden.ORCID 0000-0002-3190-1173
Rolf BreinbauerInstitute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria.ORCID 0000-0001-6009-7359
Robert KouristInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.ORCID 0000-0002-2853-3525

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cofactor-free arylmalonate decarboxylase (AMDase) is a valuable biocatalyst for synthesizing α-aryl and α-alkenyl alkanoic acids with excellent stereoselectivity. We engineered a new hydrophobic pocket in (

Indexed as

AlkenesCarboxy-LyasesMalonatesProtein EngineeringKineticsStereoisomerismSubstrate SpecificityAlkenesCarboxy-Lyasesmalonate decarboxylaseMalonatesmalonic acid

Identifiers

PMID41085469
PMCPMC12576825

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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.