ArticleThe Journal of biological chemistry2014
Substrate specificity of cytoplasmic N-glycosyltransferase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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.
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Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
- Protein β-O-glucosylation by Legionella LtpM through short consensus sequons G-T/S and S-G.Nature chemical biology · 2025Article
- Review
- Rational design of a highly activeEngineering microbiology · 2024Article
- Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.Nature communications · 2023Article
- Article
- N-glucosyltransferase GbNGT1 from ginkgo complements the auxin metabolic pathway.Horticulture research · 2021Article
- Utility of Bioluminescent Homogeneous Nucleotide Detection Assays in Measuring Activities of Nucleotide-Sugar Dependent Glycosyltransferases and Studying Their Inhibitors.Molecules (Basel, Switzerland) · 2021Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- The Legionella pneumophila Metaeffector Lpg2505 (MesI) Regulates SidI-Mediated Translation Inhibition and Novel Glycosyl Hydrolase Activity.Infection and immunity · 2020Article
- OleD Loki as a Catalyst for Hydroxamate Glycosylation.Chembiochem : a European journal of chemical biology · 2020Article
- Sequential Glycosylation of Proteins with Substrate-SpecificACS central science · 2020Article
- Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells.Frontiers in chemistry · 2020Review
- Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies.Nature communications · 2019Article
- Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.International journal of molecular sciences · 2019Review
- Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli.Glycobiology · 2019Review
- Legionella effector SetA as a general O-glucosyltransferase for eukaryotic proteins.Nature chemical biology · 2019Article
- Cytoplasmic glycoengineering of Apx toxin fragments in the development of Actinobacillus pleuropneumoniae glycoconjugate vaccines.BMC veterinary research · 2019Article
- Recent advances in the production of recombinant glycoconjugate vaccines.NPJ vaccines · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-Linked protein glycosylation is a very common post-translational modification that can be found in all kingdoms of life. The classical, highly conserved pathway entails the assembly of a lipid-linked oligosaccharide and its transfer to an asparagine residue in the sequon NX(S/T) of a secreted protein by the integral membrane protein oligosaccharyltransferase. A few species in the class of γ-proteobacteria encode a cytoplasmic N-glycosylation system mediated by a soluble N-glycosyltransferase (NGT). This enzyme uses nucleotide-activated sugars to modify asparagine residues with single monosaccharides. As these enzymes are not related to oligosaccharyltransferase, NGTs constitute a novel class of N-glycosylation catalyzing enzymes. To characterize the NGT-catalyzed reaction, we developed a sensitive and quantitative in vitro assay based on HPLC separation and quantification of fluorescently labeled substrate peptides. With this assay we were able to directly quantify glycopeptide formation by Actinobacillus pleuropneumoniae NGT and determine its substrate specificities: NGT turns over a number of different sugar donor substrates and allows for activation by both UDP and GDP. Quantitative analysis of peptide substrate turnover demonstrated a strikingly similar specificity as the classical, oligosaccharyltransferase-catalyzed N-glycosylation, with NX(S/T) sequons being the optimal NGT substrates.
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Registered trials
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.