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Glycopeptide Synthesis through endo ‐Glycosidase‐Catalyzed Oligosaccharide Transfer of Sugar Oxazolines: Probing Substrate Structural Requirement
Author(s) -
Zeng Ying,
Wang Jingsong,
Li Bing,
Hauser Steven,
Li Hengguang,
Wang LaiXi
Publication year - 2006
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200501196
Subject(s) - oxazoline , chemistry , moiety , endoglycosidase , disaccharide , glycopeptide , monosaccharide , oligosaccharide , substrate (aquarium) , acceptor , stereochemistry , combinatorial chemistry , enzyme , biochemistry , catalysis , oceanography , physics , antibiotics , condensed matter physics , geology
An array of sugar oxazolines was synthesized and tested as donor substrates for the Arthrobacter endo‐β‐N‐acetylglucosaminidase (Endo‐A)‐catalyzed glycopeptide synthesis. The experiments revealed that the minimum structure of the donor substrate required for Endo‐A catalyzed transglycosylation is a Manβ1→4‐GlcNAc oxazoline moiety. Replacement of the β‐ D ‐Man moiety with β‐ D ‐Glc, β‐ D ‐Gal, and β‐ D ‐GlcNAc monosaccharides resulted in the loss of substrate activity for the disaccharide oxazoline. Despite this, the enzyme could tolerate modifications such as attachment of additional sugar residues or a functional group at the 3‐ and/or 6‐positions of the β‐ D ‐Man moiety, thus allowing a successful transfer of selectively modified oligosaccharides to the peptide acceptor. On the other hand, the enzyme has a great flexibility for the acceptor portion and could take both small and large GlcNAc‐peptides as the acceptor. The studies implicate a great potential of the endoglycosidase‐catalyzed transglycosylation for constructing both natural and selectively modified glycopeptides.