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Issue 6, 2014
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Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid acceptor

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Abstract

Endo-β-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.

Graphical abstract: Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid acceptor

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Publication details

The article was received on 22 Oct 2013, accepted on 10 Dec 2013 and first published on 12 Dec 2013


Article type: Paper
DOI: 10.1039/C3OB42104J
Citation: Org. Biomol. Chem., 2014,12, 942-955
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    Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid acceptor

    Y. Tomabechi, M. A. Squire and A. J. Fairbanks, Org. Biomol. Chem., 2014, 12, 942
    DOI: 10.1039/C3OB42104J

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