Evidence map›Paper›PMID 33777250›Full record

ArticleChemCatChem2021

PQQ-dependent Dehydrogenase Enables One-pot Bi-enzymatic Enantio-convergent Biocatalytic Amination of Racemic

Somayyeh Gandomkar, Raquel Rocha, Frieda A Sorgenfrei, Lía Martínez Montero, Michael Fuchs, Wolfgang Kroutil

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ChemCatChem, 2021. 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
0.4field-weighted citation impact, top 43% of its field
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, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

6 authors at 3 institutions in 1 country.

Somayyeh GandomkarInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
Raquel RochaInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
Frieda A SorgenfreiInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
Lía Martínez MonteroInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
Michael FuchsInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
Wolfgang KroutilInstitute of Chemistry University of Graz, NAWI Graz 8010 Graz Austria.
University of Graz · ATNawi Graz · ATAustrian Centre of Industrial Biotechnology (Austria) · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The asymmetric amination of secondary racemic allylic alcohols bears several challenges like the reactivity of the bi-functional substrate/product as well as of the α,β-unsaturated ketone intermediate in an oxidation-reductive amination sequence. Heading for a biocatalytic amination cascade with a minimal number of enzymes, an oxidation step was implemented relying on a single PQQ-dependent dehydrogenase with low enantioselectivity. This enzyme allowed the oxidation of both enantiomers at the expense of iron(III) as oxidant. The stereoselective amination of the α,β-unsaturated ketone intermediate was achieved with transaminases using 1-phenylethylamine as formal reducing agent as well as nitrogen source. Choosing an appropriate transaminase, either the (

Indexed as

allylic aminesAmination of alcoholsbiocatalytic cascadePQQ dependent dehydrogenasesec-allylic alcoholstransaminases

Identifiers

PMID33777250
PMCPMC7986696
OpenAlexW3109334476

What OpenQuestion holds

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LicenceCC BY
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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.