{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schwarz F"],"funding":["Swiss National Science Foundation"],"pagination":["35267-74"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3186387"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["286(40)"],"pubmed_abstract":["N-Linked glycosylation is a frequent protein modification that occurs in all three domains of life. This process involves the transfer of a preassembled oligosaccharide from a lipid donor to asparagine side chains of polypeptides and is catalyzed by the membrane-bound oligosaccharyltransferase (OST). We characterized an alternative bacterial pathway wherein a cytoplasmic N-glycosyltransferase uses nucleotide-activated monosaccharides as donors to modify asparagine residues of peptides and proteins. N-Glycosyltransferase is an inverting glycosyltransferase and recognizes the NX(S/T) consensus sequence. It therefore exhibits similar acceptor site specificity as eukaryotic OST, despite the unrelated predicted structural architecture and the apparently different catalytic mechanism. The identi"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence."],"pmcid":["PMC3186387"],"funding_grant_id":["105541"],"pubmed_authors":["Aebi M","Fan YY","Schubert M","Schwarz F"],"additional_accession":[]},"is_claimable":false,"name":"Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence.","description":"N-Linked glycosylation is a frequent protein modification that occurs in all three domains of life. This process involves the transfer of a preassembled oligosaccharide from a lipid donor to asparagine side chains of polypeptides and is catalyzed by the membrane-bound oligosaccharyltransferase (OST). We characterized an alternative bacterial pathway wherein a cytoplasmic N-glycosyltransferase uses nucleotide-activated monosaccharides as donors to modify asparagine residues of peptides and proteins. N-Glycosyltransferase is an inverting glycosyltransferase and recognizes the NX(S/T) consensus sequence. It therefore exhibits similar acceptor site specificity as eukaryotic OST, despite the unrelated predicted structural architecture and the apparently different catalytic mechanism. The identi","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Oct","modification":"2025-05-29T20:29:15.115Z","creation":"2025-05-29T20:29:15.115Z"},"accession":"S-EPMC3186387","cross_references":{"pubmed":["21852240"],"doi":["10.1074/jbc.M111.277160","10.1074/jbc.m111.277160"]}}