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N‐Glycosylation with Synthetic Undecaprenyl Pyrophosphate‐Linked Oligosaccharide to Oligopeptides by PglB Oligosaccharyltransferase from Campylobacter jejuni
Author(s) -
Ishiwata Akihiro,
Taguchi Yuya,
Lee Yong Joo,
Watanabe Taisuke,
Kohda Daisuke,
Ito Yukishige
Publication year - 2015
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.201402658
Subject(s) - campylobacter jejuni , glycosylation , chemistry , pyrophosphate , oligopeptide , biochemistry , residue (chemistry) , stereochemistry , peptide , biology , bacteria , enzyme , genetics
The oligosaccharyltransferase PglB from Campylobacter jejuni catalyses the N ‐glycosylation reaction with undecaprenyl‐pyrophosphate‐linked Glc 1 GalNAc 5 Bac 1 (Und‐PP‐Glc 1 GalNAc 5 Bac 1 ). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und‐PP‐Bac 1 and Und‐PP‐GalNAc 2 Bac 1 are transferred efficiently to the Asn residue in the consensus sequence (D/E‐X′‐N‐X‐T/S, X′,X≠P). The products were analyzed in detail by tandem MS to confirm their chemical structures.