Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 7, Issue 15, Pages 3128-3140Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b907273j
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- University of Kagawa
- University of York
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The synthesis of a truncated complex N-glycan hexasaccharide oxazoline was achieved producing a substrate that was assayed as an activated donor for glycosylation catalysed by the endohexosaminidases Endo A and Endo M. For Endo M competitive product hydrolysis was seen to limit synthetic efficiency. In spite of its natural hydrolytic selectivity wild type Endo A was able to process the truncated complex N-glycan oxazoline, albeit with limited synthetic efficiency; notably the product was not a substrate for Endo A catalysed hydrolysis. Two Endo A mutants, E173Q and E173H, were also assayed, but were unable to process this oxazoline.
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