Structural and kinetic dissection of the endo-α-1,2-mannanase activity of bacterial GH99 glycoside hydrolases from Bacteroides spp

Z Hakki; AJ Thompson; S Bellmaine; G Speciale; GJ Davies; SJ Williams

Journal article

Structural and kinetic dissection of the endo-α-1,2-mannanase activity of bacterial GH99 glycoside hydrolases from Bacteroides spp

Z Hakki, AJ Thompson, S Bellmaine, G Speciale, GJ Davies, SJ Williams

Chemistry (Weinheim an der Bergstrasse, Germany) | WILEY-V C H VERLAG GMBH | Published : 2015

DOI: 10.1002/chem.201405539

Abstract

© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.Glycoside hydrolase family 99 (GH99) was created to categorize sequence-related glycosidases possessing endo-α-mannosidase activity: the cleavage of mannosidic linkages within eukaryotic N-glycan precursors (Glc1-3 Man9 GlcNAc2 ), releasing mono-, di- and triglucosylated-mannose (Glc1-3 -1,3-Man). GH99 family members have recently been implicated in the ability of Bacteroides spp., present within the gut microbiota, to metabolize fungal cell wall α-mannans, releasing α-1,3-mannobiose by hydrolysing αMan-1,3-αMan→1,2-αMan-1,2-αMan sequences within branches off the main α-1,6-mannan backbone. We report the development of a series of substrates ..

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University of Melbourne Researchers

Spencer Williams Author

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Grants

Funding Acknowledgements

We thank the Australian Research Council (ARC), the UK Biotechnology and Biological Sciences Research Council (BB/G016127/1) and the European Research Council (ERC-2012-AdG-322942) for grant support. S.J.W. is an ARC Future Fellow. Z.H. was supported by a travelling fellowship from the European Molecular Biology Organization. The staff of the Diamond Light Source (Didcot, UK) are thanked for the provision of beamline and X-ray data collection facilities.