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Unusual Transglycosylation Activity of Flavobacterium meningosepticum Endoglycosidases Enables Convergent Chemoenzymatic Synthesis of Core Fucosylated Complex N‐Glycopeptides
Author(s) -
Huang Wei,
Li Jie,
Wang LaiXi
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000763
Subject(s) - glycopeptide , fucose , flavobacterium , chemistry , sialic acid , glycan , stereochemistry , endoglycosidase , biochemistry , glycosidic bond , glycoprotein , enzyme , biology , bacteria , pseudomonas , genetics , antibiotics
Structurally well defined, homogeneous glycopeptides and glycoproteins are indispensable tools for functional glycomics studies. By screening of various endo ‐β‐ N ‐acetylglucosaminidases through the use of appropriate synthetic donor and acceptor substrates, we have found that the Flavobacterium meningosepticum endo ‐β‐ N ‐acetyl‐glucosaminidases (GH family 18), including Endo‐F2 and Endo‐F3, were able to glycosylate α‐1,6‐fucosylated GlcNAc derivative to provide natural, corefucosylated complex‐type N‐glycopeptides. The Endo‐F2 and Endo‐F3 were efficient for transferring both sialylated and asialylated glycans and were highly specific for an α‐1,6‐fucosylated GlcNAc‐peptide as acceptor for transglycosylation, showing only marginal activity with non‐fucosylated GlcNAc‐peptides. In contrast, we found that the commonly used endoglycosidases such as Endo‐A and Endo‐M, which belong to GH family 85, were unable to take α‐1,6‐fucosyl‐GlcNAc derivative as acceptors for transglycosylation. The novel activity of Endo‐F2 and Endo‐F3 was successfully applied for a highly convergent chemoenzymatic synthesis of a full‐sized CD52 glycopeptide antigen carrying both terminal sialic acid and core fucose. This is the first report on endoglycosidases that are able to glycosylate α‐1,6‐fucosylated GlcNAc derivatives to form natural core‐fucosylated glycopeptides.