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

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JournalChemical Communications
DateAccepted/In press - 10 Aug 2016
DateE-pub ahead of print - 15 Aug 2016
DatePublished (current) - 25 Sep 2016
Issue number74
Volume52
Number of pages4
Pages (from-to)11096-11099
Early online date15/08/16
Original languageEnglish

Abstract

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.

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©The Royal Society of Chemistry 2016.

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