Evidence map›Paper›PMID 32347609›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020

Folding Assessment of Incorporation of Noncanonical Amino Acids Facilitates Expansion of Functional-Group Diversity for Enzyme Engineering.

Ivana Drienovská, Matúš Gajdoš, Alexia Kindler, Mahsa Takhtehchian, Barbara Darnhofer, Ruth Birner-Gruenberger, Mark Dörr, Uwe T Bornscheuer, Robert Kourist

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 9 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

9 authors at 4 institutions in 2 countries.

Ivana DrienovskáInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.ORCID http://orcid.org/0000-0003-1715-4236
Matúš GajdošInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.
Alexia KindlerInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.
Mahsa TakhtehchianInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.
Barbara DarnhoferDiagnostic and Research Institute of Patholoy, Diagnostic and Research Center of Molecular Medicine, Medical University of Graz, Neue Stiftingtalstraße 6, 8010, Graz, Austria.
Ruth Birner-GruenbergerDiagnostic and Research Institute of Patholoy, Diagnostic and Research Center of Molecular Medicine, Medical University of Graz, Neue Stiftingtalstraße 6, 8010, Graz, Austria.
Mark DörrBiotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.
Uwe T BornscheuerBiotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0003-0685-2696
Robert KouristInstitute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.ORCID http://orcid.org/0000-0002-2853-3525
Institute of Molecular Biotechnology · ATUniversitätsmedizin Greifswald · DEMedical University of Graz · ATTU Wien · AT

Funding

TU Graz, Internationale Beziehungen und Mobilitätsprogramme Competetive Funding Programme
6 · The paper itself

Abstract

Protein design is limited by the diversity of functional groups provided by the canonical protein "building blocks". Incorporating noncanonical amino acids (ncAAs) into enzymes enables a dramatic expansion of their catalytic features. For this, quick identification of fully translated and correctly folded variants is decisive. Herein, we report the engineering of the enantioselectivity of an esterase utilizing several ncAAs. Key for the identification of active and soluble protein variants was the use of the split-GFP method, which is crucial as it allows simple determination of the expression levels of enzyme variants with ncAA incorporations by fluorescence. Several identified variants led to improved enantioselectivity or even inverted enantiopreference in the kinetic resolution of ethyl 3-phenylbutyrate.

Indexed as

Amino AcidsProtein EngineeringCatalysisEsterasesProteinsAmino AcidsEsterasesProteinsbiocatalysisenzyme expressionnoncanonical amino acidsprotein engineeringpseudomonas fluorescens esterase

Identifiers

PMID32347609
PMCPMC7590180
OpenAlexW3020023536

What OpenQuestion holds

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LicenceCC BY
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.