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An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling.

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 fuco...

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Publication status:
Published
Peer review status:
Peer Reviewed

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Publisher copy:
10.1021/ja301334b

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Institution:
University of Oxford
Department:
Department of Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Department of Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Department of Biochemistry
Role:
Author
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Funding agency for:
Goodfellow, JJ
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Funding agency for:
Yamamoto, K
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Funding agency for:
Bonomelli, C
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Funding agency for:
Krishna, B
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Journal:
Journal of the American Chemical Society
Volume:
134
Issue:
19
Pages:
8030-8033
Publication date:
2012-05-02
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:cf92f6dc-e3d3-4eee-b0c3-188ce9feba49
Source identifiers:
329007
Local pid:
pubs:329007

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