Evidence map›Paper›PMID 35713203›Full record

ArticleChembiochem : a European journal of chemical biology2022

Recombinant l-Amino Acid Oxidase with Broad Substrate Spectrum for Co-substrate Recycling in (S)-Selective Transaminase-Catalyzed Kinetic Resolutions.

Tobias Heinks, Jannik Paulus, Simon Koopmeiners, Tobias Beuel, Norbert Sewald, Matthias Höhne, Uwe T Bornscheuer, Gabriele Fischer von Mollard

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

Article in Chembiochem : a European journal of chemical biology, 2022. 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
0.6field-weighted citation impact, top 36% 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.

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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

8 authors at 3 institutions in 1 country.

Tobias HeinksFaculty of Chemistry, Biochemistry, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID 0000-0003-3131-2106
Jannik PaulusFaculty of Chemistry, Organic and Bioorganic Chemistry, Bielefeld University, Universitätsstraße 25, 33615, Bielefeld, Germany.
Simon KoopmeinersFaculty of Chemistry, Biochemistry, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.
Tobias BeuelFaculty of Chemistry, Biochemistry, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.
Norbert SewaldFaculty of Chemistry, Organic and Bioorganic Chemistry, Bielefeld University, Universitätsstraße 25, 33615, Bielefeld, Germany.ORCID 0000-0002-0309-2655
Matthias HöhneProtein Biochemistry, Institute of Biochemistry, University of Greifswald, Felix Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID 0000-0002-2542-725X
Uwe T BornscheuerDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID 0000-0003-0685-2696
Gabriele Fischer von MollardFaculty of Chemistry, Biochemistry, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID 0000-0003-3236-1401
Bielefeld University · DEUniversität Greifswald · DEUniversitätsmedizin Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chiral and enantiopure amines can be produced by enantioselective transaminases via kinetic resolution of amine racemates. This transamination reaction requires stoichiometric amounts of co-substrate. A dual-enzyme recycling system overcomes this limitation: l-amino acid oxidases (LAAO) recycle the accumulating co-product of (S)-selective transaminases in the kinetic resolution of racemic amines to produce pure (R)-amines. However, availability of suitable LAAOs is limited. Here we use the heterologously produced, highly active fungal hcLAAO4 with broad substrate spectrum. H

Indexed as

L-Amino Acid OxidaseTransaminasesAminesCatalysisOxidoreductasesStereoisomerismSubstrate SpecificityAminesL-Amino Acid OxidaseOxidoreductasesTransaminasesbiocatalysisco-substrate recyclingenantiopure (R)-amineskinetic resolutionl-amino acid oxidase (LAAO)transaminases

Identifiers

PMID35713203
PMCPMC9543090
OpenAlexW4283028062

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.