Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-β-galactosaminidase that uses neighbouring group participation

C. Roth, M. Petricevic, A. John, E. D. Goddard-Borger*, G. J. Davies, S. J. Williams

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Bacteroides vulgatus is a member of the human microbiota whose abundance is increased in patients with Crohn's disease. We show that a B. vulgatus glycoside hydrolase from the carbohydrate active enzyme family GH123, BvGH123, is an N-acetyl-β-galactosaminidase that acts with retention of stereochemistry, and, through a 3-D structure in complex with Gal-thiazoline, provide evidence in support of a neighbouring group participation mechanism.

Original languageEnglish
Pages (from-to)11096-11099
Number of pages4
JournalChemical Communications
Issue number74
Early online date15 Aug 2016
Publication statusPublished - 25 Sept 2016

Bibliographical note

©The Royal Society of Chemistry 2016.

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