Abstract
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.
Original language | English |
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Pages (from-to) | 3128-3140 |
Number of pages | 13 |
Journal | Organic and Biomolecular Chemistry |
Volume | 7 |
Issue number | 15 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- STIMULATING PROTEIN NESP
- CHEMOENZYMATIC SYNTHESIS
- LINKED OLIGOSACCHARIDES
- GLYCOPROTEIN-SYNTHESIS
- ALLYL ETHERS
- TRANSGLYCOSYLATION ACTIVITY
- ACETYLGLUCOSAMINE MOIETIES
- ARTHROBACTER PROTOPHORMIAE
- HUMAN-ERYTHROPOIETIN
- MILD CONDITIONS