Evidence map›Paper›PMID 33527702›Full record

ArticleChembiochem : a European journal of chemical biology2021

Production of the Carboxylate Reductase from Nocardia otitidiscaviarum in a Soluble, Active Form for in vitro Applications.

Douglas Weber, David Patsch, Annika Neumann, Margit Winkler, Dörte Rother

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

Douglas WeberInstitute of Bio- and Geosciences (IBG-1), Biotechnology Forschungszentrum Jülich GmbH, Leo-Brandt-Str. 1, 52425, Jülich, Germany.
David PatschInstitute of Bio- and Geosciences (IBG-1), Biotechnology Forschungszentrum Jülich GmbH, Leo-Brandt-Str. 1, 52425, Jülich, Germany.
Annika NeumannInstitute of Bio- and Geosciences (IBG-1), Biotechnology Forschungszentrum Jülich GmbH, Leo-Brandt-Str. 1, 52425, Jülich, Germany.
Margit Winkleracib-Austrian Centre of Industrial Biotechnology, Petersgasse14, 8010, Graz, Austria.
Dörte RotherInstitute of Bio- and Geosciences (IBG-1), Biotechnology Forschungszentrum Jülich GmbH, Leo-Brandt-Str. 1, 52425, Jülich, Germany.ORCID 0000-0002-2339-4431
Forschungszentrum Jülich · DEInstitute of Molecular Biotechnology · AT

Funding

University of Freiburg, Germany
6 · The paper itself

Abstract

Accessing aldehydes from carboxylate moieties is often a challenging task. In this regard, carboxylate reductases (CARs) are promising catalysts provided by nature that are able to accomplish this task in just one step, avoiding over-reduction to the alcohol product. However, the heterologous expression of CARs can be quite difficult due to the excessive formation of insoluble protein, thus hindering further characterization and application of the enzyme. Here, the heterologous production of the carboxylate reductase from Nocardia otitidiscaviarum (NoCAR) was optimized by a combination of i) optimized cultivation conditions, ii) post-translational modification with a phosphopantetheinyl transferase and iii) selection of an appropriate expression strain. Especially, the selection of Escherichia coli tuner cells as host had a strong effect on the final 110-fold increase in the specific activity of NoCAR. This highly active NoCAR was used to reduce sodium benzoate to benzaldehyde, and it was successfully assembled with an in vitro regeneration of ATP and NADPH, being capable of reducing about 30 mM sodium benzoate with high selectivity in only 2 h of reaction.

Indexed as

Aldehyde OxidoreductasesBacterial ProteinsEscherichia coliNADPNocardiaOxidation-ReductionRecombinant ProteinsSodium BenzoateSolubilityAldehyde OxidoreductasesBacterial ProteinsNADPRecombinant ProteinsSodium Benzoatealdehydescarboxylate reductaseinclusion bodiesin vitro cofactor regenerationsoluble protein

Identifiers

PMID33527702
PMCPMC8251736
OpenAlexW3126305796

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.