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Cited by 41Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisChemical Reaction Mechanisms

A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2

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Gómez, Hansel, Rojas, Raúl, Patel, Divya, Tabak, Lawrence A., Lluch, José M., Masgrau, Laura·2014·Org. Biomol. Chem.
DOI 10.1039/c3ob42569jPMC PMC4744471
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Abstract

GalNAc-T2 catalyses GalNAc O-glycosylation via a front-side nucleophilic attack in which stabilization of the UDP leaving group is crucial.

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  • UDP-galactose has been postulated as an alternative sugar substrate for GalNAc-T2.

    “Although UDP-galactose has been postulated as an alternative sugar substrate for GalNAc-T2 [21, 30], no sugar moieties attached to T7Muc10, which correlate with galactose residues were detected.”

    From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [30]

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Authors
Gómez, H., Rojas, R., Patel, D., Tabak, L. A., Lluch, J. M., & Masgrau, L.
Affiliations
  • Universitat Autònoma de Barcelona (ES)
  • National Institutes of Health (US)
Corresponding author
  • Tabak, Lawrence A.
  • Masgrau, Laura
ORCID
Venue
Org. Biomol. Chem.
Publisher
Royal Society of Chemistry (RSC)
Published
2014
Volume
12
Issue
17
Pages
2645-2655
ISSN
  • 1477-0520 (ISSN-L)
  • 1477-0539
DOI
10.1039/c3ob42569j
PMC
PMC4744471
OpenAlex
W2080780084
Cited by
41
References
2
Citations by year
2025: 2 · 2024: 1 · 2022: 3 · 2021: 5 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 8 · 2015: 6 · 2014: 7
FWCI
3.41
Type
journal article
Language
en
Open access
Locations
  • Organic & Biomolecular Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Generalitat de Catalunya
  • Ministerio de Economía y Competitividad
  • National Institutes of Health
  • National Institute of Dental and Craniofacial Research (ZIADE000739)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Keywords
O-glycosylation, mucin-type O-glycans, QM/MM calculations, enzyme mechanism, transition state stabilization, site-directed mutagenesis, glycosyltransferase substrate specificity
MeSH terms
Polypeptide N-acetylgalactosaminyltransferase, Catalysis, Glycosylation, Humans, Hydrogen Bonding, Kinetics, Models, Molecular, Mucins, Polysaccharides, Protein Conformation, Quantum Theory, Substrate Specificity, Uridine Diphosphate, N-Acetylgalactosaminyltransferases, Computational Biology

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