{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Makrydaki E"],"funding":["RCUK | Engineering and Physical Sciences Research Council (EPSRC)","RCUK | Biotechnology and Biological Sciences Research Council","RCUK | Engineering and Physical Sciences Research Council","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["732-741"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11142912"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(6)"],"pubmed_abstract":["Glycosylation is a critical post-translational protein modification that affects folding, half-life and functionality. Glycosylation is a non-templated and heterogeneous process because of the promiscuity of the enzymes involved. We describe a platform for sequential glycosylation reactions for tailored sugar structures (SUGAR-TARGET) that allows bespoke, controlled N-linked glycosylation in vitro enabled by immobilized enzymes produced with a one-step immobilization/purification method. We reconstruct a reaction cascade mimicking a glycosylation pathway where promiscuity naturally exists to humanize a range of proteins derived from different cellular systems, yielding near-homogeneous glycoforms. Immobilized β-1,4-galactosyltransferase is used to enhance the galactosylation profile of thr"],"journal":["Nature chemical biology"],"pubmed_title":["Immobilized enzyme cascade for targeted glycosylation."],"pmcid":["PMC11142912"],"funding_grant_id":["EP/N509486/1","BB/P02789X/1","EP/K038648/1, EP/H04986X/1 and EP/K038648/1","EP/H04986X/1"],"pubmed_authors":["Donini R","Makrydaki E","Kuntz DA","Royle K","Rose DR","Moya Ramirez I","Polizzi KM","Kontoravdi C","Krueger A","Haslam SM"],"additional_accession":[]},"is_claimable":false,"name":"Immobilized enzyme cascade for targeted glycosylation.","description":"Glycosylation is a critical post-translational protein modification that affects folding, half-life and functionality. Glycosylation is a non-templated and heterogeneous process because of the promiscuity of the enzymes involved. We describe a platform for sequential glycosylation reactions for tailored sugar structures (SUGAR-TARGET) that allows bespoke, controlled N-linked glycosylation in vitro enabled by immobilized enzymes produced with a one-step immobilization/purification method. We reconstruct a reaction cascade mimicking a glycosylation pathway where promiscuity naturally exists to humanize a range of proteins derived from different cellular systems, yielding near-homogeneous glycoforms. Immobilized β-1,4-galactosyltransferase is used to enhance the galactosylation profile of thr","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-04-29T14:12:14.267Z","creation":"2026-04-14T03:06:54.834Z"},"accession":"S-EPMC11142912","cross_references":{"pubmed":["38321209"],"doi":["10.1038/s41589-023-01539-4"]}}