N‐Glycosylation with Synthetic Undecaprenyl Pyrophosphate‐Linked Oligosaccharide to Oligopeptides by PglB Oligosaccharyltransferase from Campylobacter jejuni. Issue 5 (16th February 2015)

• Record Type: Journal Article
• Authors: Ishiwata, Akihiro; Taguchi, Yuya; Lee, Yong Joo; Watanabe, Taisuke; Kohda, Daisuke; Ito, Yukishige
• Is Part Of: Chembiochem. Volume 16:Issue 5(2015)
• Page Start: 731
• Page End: 737
• Publication Date: 2015-02-16
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201402658
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>The oligosaccharyltransferase PglB from <italic>Campylobacter jejuni</italic> catalyses the <italic>N</italic>‐glycosylation reaction with undecaprenyl‐pyrophosphate‐linked Glc₁GalNAc₅Bac₁ (Und‐PP‐Glc₁GalNAc₅Bac₁). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und‐PP‐Bac₁ and Und‐PP‐GalNAc₂Bac₁ 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.</p> </abstract>