Evidence map›Paper›PMID 36846821›Full record

ArticleACS catalysis2023

Mechanistic Insights into the Ene-Reductase-Catalyzed Promiscuous Reduction of Oximes to Amines.

Willem B Breukelaar, Nakia Polidori, Amit Singh, Bastian Daniel, Silvia M Glueck, Karl Gruber, Wolfgang Kroutil

Abstract read
In one paragraph

Article in ACS catalysis, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
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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.

Willem B BreukelaarDepartment of Chemistry, NAWI Graz, University of Graz, Heinrichstraße 28, 8010 Graz, Austria.
Nakia PolidoriInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010 Graz, Austria.ORCID https://orcid.org/0000-0003-0361-3091
Amit SinghInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010 Graz, Austria.
Bastian DanielInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010 Graz, Austria.
Silvia M GlueckDepartment of Chemistry, NAWI Graz, University of Graz, Heinrichstraße 28, 8010 Graz, Austria.ORCID https://orcid.org/0000-0003-2154-7585
Karl GruberInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010 Graz, Austria.ORCID https://orcid.org/0000-0002-3485-9740
Wolfgang KroutilDepartment of Chemistry, NAWI Graz, University of Graz, Heinrichstraße 28, 8010 Graz, Austria.ORCID https://orcid.org/0000-0002-2151-6394

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biocatalytic reduction of the oxime moiety to the corresponding amine group has only recently been found to be a promiscuous activity of ene-reductases transforming α-oximo β-keto esters. However, the reaction pathway of this two-step reduction remained elusive. By studying the crystal structures of enzyme oxime complexes, analyzing molecular dynamics simulations, and investigating biocatalytic cascades and possible intermediates, we obtained evidence that the reaction proceeds

Identifiers

PMID36846821
PMCPMC9942197

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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.