Evidence map›Paper›PMID 32978392›Full record

ArticleNature communications2020

Thioglycoligase derived from fungal GH3 β-xylosidase is a multi-glycoligase with broad acceptor tolerance.

Manuel Nieto-Domínguez, Beatriz Fernández de Toro, Laura I de Eugenio, Andrés G Santana, Lara Bejarano-Muñoz, Zach Armstrong, Juan Antonio Méndez-Líter, Juan Luis Asensio, Alicia Prieto, Stephen G Withers and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

10 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Family 1 Glycosyltransferase UGT706F8 fromACS sustainable chemistry & engineering · 2022
    Article
  7. Review
  8. Article
  9. Lytic Polysaccharide Monooxygenase fromInternational journal of molecular sciences · 2021
    Article
  10. Fungal glycosyl hydrolases for sustainable plant biomass valorization: Talaromyces amestolkiae as a model fungus.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Review
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

12 authors at 3 institutions in 2 countries.

Manuel Nieto-DomínguezBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain. mnietdom@gmail.com.ORCID http://orcid.org/0000-0001-8192-5176
Beatriz Fernández de ToroNMR and Molecular Recognition Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.
Laura I de EugenioBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.
Andrés G SantanaGlycochemistry and Molecular recognition group, Instituto de Química Orgánica General (CSIC), C/Juan de la Cierva, 3, 28006, Madrid, Spain.
Lara Bejarano-MuñozBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.ORCID http://orcid.org/0000-0002-8242-8523
Zach ArmstrongDepartment of Chemistry, Centre for High-Throughput Biology, University of British Columbia, Vancouver, Canada.ORCID http://orcid.org/0000-0002-4086-2946
Juan Antonio Méndez-LíterBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.
Juan Luis AsensioGlycochemistry and Molecular recognition group, Instituto de Química Orgánica General (CSIC), C/Juan de la Cierva, 3, 28006, Madrid, Spain.
Alicia PrietoBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.
Stephen G WithersDepartment of Chemistry, Centre for High-Throughput Biology, University of British Columbia, Vancouver, Canada.ORCID http://orcid.org/0000-0002-6722-5701
Francisco Javier CañadaNMR and Molecular Recognition Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain.ORCID http://orcid.org/0000-0003-4462-1469
María Jesús MartínezBiotechnology for Lignocellulosic Biomass Group, Centro de Investigaciones Biológicas Margarita Salas (CSIC), C/Ramiro de Maeztu 9, 28040, Madrid, Spain. mjmartinez@cib.csic.es.ORCID http://orcid.org/0000-0003-2166-1097
Centro de Investigaciones Biológicas Margarita Salas · ESInstituto de Química Orgánica General · ESUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of customized glycoconjugates constitutes a major goal for biocatalysis. To this end, engineered glycosidases have received great attention and, among them, thioglycoligases have proved useful to connect carbohydrates to non-sugar acceptors. However, hitherto the scope of these biocatalysts was considered limited to strong nucleophilic acceptors. Based on the particularities of the GH3 glycosidase family active site, we hypothesized that converting a suitable member into a thioglycoligase could boost the acceptor range. Herein we show the engineering of an acidophilic fungal β-xylosidase into a thioglycoligase with broad acceptor promiscuity. The mutant enzyme displays the ability to form O-, N-, S- and Se- glycosides together with sugar esters and phosphoesters with conversion yields from moderate to high. Analyses also indicate that the pK

Indexed as

BiocatalysisCatalytic DomainDrug ToleranceFungiGlycoconjugatesGlycoside HydrolasesGlycosidesGlycosylationHydrogen-Ion ConcentrationKineticsModels, MolecularMutagenesisSubstrate SpecificityTalaromycesXylosidasesexo-1,4-beta-D-xylosidaseGlycoconjugatesGlycoside HydrolasesGlycosidesXylosidases

Identifiers

PMID32978392
PMCPMC7519651
OpenAlexW3088244240

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.