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• W2293739757 endingPage "9370" @default.
• W2293739757 startingPage "9356" @default.
• W2293739757 abstract "Chemoenzymatic synthesis is emerging as a promising approach to the synthesis of homogeneous glycopeptides and glycoproteins highly demanded for functional glycomics studies, but its generality relies on the availability of a range of enzymes with high catalytic efficiency and well defined substrate specificity. We describe in this paper the discovery of glycosynthase mutants derived from Elizabethkingia meningoseptica endoglycosidase F3 (Endo-F3) of the GH18 family, which are devoid of the inherent hydrolytic activity but are able to take glycan oxazolines for transglycosylation. Notably, the Endo-F3 D165A and D165Q mutants demonstrated high acceptorsubstrate specificity toward α1,6-fucosyl-GlcNAc-Asn or α1,6-fucosyl-GlcNAc-polypeptide in transglycosylation, enabling a highly convergent synthesis of core-fucosylated, complex CD52 glycopeptide antigen. The Endo-F3 mutants were able to use both bi- and triantennary glycan oxazolines as substrates for transglycosylation, in contrast to previously reported endoglycosidases derived from Endo-S, Endo-M, Endo-D, and Endo-A mutants that could not recognize triantennary N-glycans. Using rituximab as a model system, we have further demonstrated that the Endo-F3 mutants are highly efficient for glycosylation remodeling of monoclonal antibodies to produce homogeneous intact antibody glycoforms. Interestingly, the new triantennary glycan glycoform of antibody showed much higher affinity for galectin-3 than that of the commercial antibody. The Endo-F3 mutants represent the first endoglycosidase-based glycosynthases capable of transferring triantennary complex N-glycans, which would be very useful for glycoprotein synthesis and glycosylation remodeling of antibodies." @default.
• W2293739757 created "2016-06-24" @default.
• W2293739757 creator A5036627086 @default.
• W2293739757 creator A5039183493 @default.
• W2293739757 creator A5058258557 @default.
• W2293739757 creator A5088125489 @default.
• W2293739757 date "2016-04-01" @default.
• W2293739757 modified "2023-10-10" @default.
• W2293739757 title "Endo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins" @default.
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• W2293739757 doi "https://doi.org/10.1074/jbc.m116.721597" @default.
• W2293739757 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4861498" @default.
• W2293739757 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26966183" @default.
• W2293739757 hasPublicationYear "2016" @default.
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