Evidence map›Paper›PMID 31652818›Full record

ReviewInternational journal of molecular sciences2019

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.

Luuk Mestrom, Marta Przypis, Daria Kowalczykiewicz, André Pollender, Antje Kumpf, Stefan R Marsden, Isabel Bento, Andrzej B Jarzębski, Katarzyna Szymańska, Arkadiusz Chruściel and 4 more

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Article
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  11. Article
  12. Review
  13. Enzymatic Glycosylation ofBiomolecules · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. 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

14 authors.

Luuk MestromDepartment of Biotechnology, Delft University of Technology, Section Biocatalysis, Van der Maasweg 9, 2629 HZ Delft, The Netherlands. l.mestrom@tudelft.nl.
Marta PrzypisDepartment of Organic Chemistry, Bioorganic Chemistry and Biotechnology, Silesian University of Technology, B. Krzywoustego 4, 44-100 Gliwice, Poland. marta.przypis@polsl.pl.
Daria KowalczykiewiczDepartment of Organic Chemistry, Bioorganic Chemistry and Biotechnology, Silesian University of Technology, B. Krzywoustego 4, 44-100 Gliwice, Poland. daria.kowalczykiewicz@polsl.pl.
André PollenderEnvironmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany. andre.pollender@ioez.tu-freiberg.de.
Antje KumpfEnvironmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany. antje.kumpf@ruhr-uni-bochum.de.
Stefan R MarsdenDepartment of Biotechnology, Delft University of Technology, Section Biocatalysis, Van der Maasweg 9, 2629 HZ Delft, The Netherlands. s.r.marsden@tudelft.nl.
Isabel BentoEMBL Hamburg, Notkestraβe 85, 22607 Hamburg, Germany. ibento@embl-hamburg.de.
Andrzej B JarzębskiInstitute of Chemical Engineering, Polish Academy of Sciences, Bałtycka 5, 44-100 Gliwice, Poland. andrzej.jarzebski@polsl.pl.
Katarzyna SzymańskaDepartment of Chemical and Process Engineering, Silesian University of Technology, Ks. M. Strzody 7, 44-100 Gliwice, Poland. katarzyna.szymanska@polsl.pl.
Arkadiusz ChruścielMEXEO Wiesław Hreczuch, ul. Energetyków 9, 47-225 Kędzierzyn-Koźle, Poland. arkach@mexeo.pl.
Dirk TischlerEnvironmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany. dirk.tischler@rub.de.
Rob SchoevaartChiralVision, J.H. Oortweg 21, 2333 CH Leiden, The Netherlands. schoevaart@chiralvision.com.
Ulf HanefeldDepartment of Biotechnology, Delft University of Technology, Section Biocatalysis, Van der Maasweg 9, 2629 HZ Delft, The Netherlands. u.hanefeld@tudelft.nl.
Peter-Leon HagedoornDepartment of Biotechnology, Delft University of Technology, Section Biocatalysis, Van der Maasweg 9, 2629 HZ Delft, The Netherlands. p.l.hagedoorn@tudelft.nl.

Funding

ERA IB ERA-IB-15-110
6 · The paper itself

Abstract

Enzymes are nature's catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.

Indexed as

BiocatalysisChemistry Techniques, SyntheticGlycoconjugatesGlycosyltransferasesGlycoconjugatesGlycosyltransferasesapplied biocatalysiscarbohydratechemoenzymatic synthesisenzyme cascadesglycosyltransferaseLeloirnucleotidesugar chemistry

Identifiers

PMID31652818
PMCPMC6861944

What OpenQuestion holds

Textmetadata
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.