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J Am Chem Soc. 2012 May 16;134(19):8030-3. doi: 10.1021/ja301334b. Epub 2012 May 2.

An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling.

Author information

1
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.

Abstract

Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes , EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.

PMID:
22551167
DOI:
10.1021/ja301334b
[Indexed for MEDLINE]

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