Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 12, Issue 6, Pages 942-955Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3ob42104j
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Funding
- Royal Society of New Zealand Marsden Fund [UOC0910]
- Biomolecular Interaction Centre (BIC) at the University of Canterbury
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Endo-beta-N-Acetylglucosaminidases (ENGases) are highly useful biocatalysts that can be used to synthetically access a wide variety of defined homogenous N-linked glycoconjugates in a convergent manner. The synthetic efficiency of a selection of family GH85 ENGases was investigated as the structure of the acceptor substrate was varied. Several different GlcNAc-asparagine acceptors were synthesised, and used in conjunction with penta-and decasaccharide oxazoline donors. Different enzymes showed different tolerances of modification of the GlcNAc acceptor. Whilst none tolerated modification of either the 4- or 6-hydroxyl, both Endo M and Endo D tolerated modification of OH-3. For Endo D the achievable synthetic efficiency was increased by a factor of three by the use a 3-O-benzyl protected acceptor. The presence of a fucose at position-3 was not tolerated by any of the enzymes assayed.
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