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Issue 8, 2010
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Streptococcus pneumoniae endohexosaminidase D; feasibility of using N-glycan oxazoline donors for synthetic glycosylation of a GlcNAc-asparagine acceptor

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Abstract

Endohexosaminidase D, a family 85 glycoside hydrolase from S. pneumoniae and the first endohexosaminidase to be discovered, is found to be capable of catalysing the glycosylation of a glycosyl amino acid bearing a GlcNAc residue using a variety of N-glycan oxazoline donors. Although enzyme-catalysed oxazoline hydrolysis is a significant competing reaction that is not countered by the addition of organic co-solvents or variation of reaction pH, a high yielding synthetic process can be achieved by the sequential addition of multiple equivalents of oxazoline donor, demonstrating the synthetic potential of this enzyme as a biocatalyst for the synthesis of defined glycoconjugates. Notably Endo-D does not appear to hydrolyse the resulting products under the conditions used. The synthetic activity displayed by Endo D implies that other, as yet untested, family GH85 enzymes may display similar synthetic potential. Furthermore since Endo D is capable of cleaving N-glycans attached to monoclonal antibodies (mAbs), and also of cleaving glycans that are core-fucosylated, the development of Endo D as a useful biocatalyst for the synthesis of important defined homogeneous complex glycoconjugates may have significant future potential, provided that the limitation of direct oxazoline hydrolysis can be surmounted.

Graphical abstract: Streptococcus pneumoniae endohexosaminidase D; feasibility of using N-glycan oxazoline donors for synthetic glycosylation of a GlcNAc-asparagine acceptor

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Supplementary files

Article information


Submitted
10 Dec 2009
Accepted
04 Feb 2010
First published
25 Feb 2010

Org. Biomol. Chem., 2010,8, 1861-1869
Article type
Paper

Streptococcus pneumoniae endohexosaminidase D; feasibility of using N-glycan oxazoline donors for synthetic glycosylation of a GlcNAc-asparagine acceptor

T. B. Parsons, M. K. Patel, A. B. Boraston, D. J. Vocadlo and A. J. Fairbanks, Org. Biomol. Chem., 2010, 8, 1861
DOI: 10.1039/B926078A

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