Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-beta-galactosaminidase that uses neighbouring group participation
- Author(s)
- Roth, C; Petricevic, M; John, A; Goddard-Borger, ED; Davies, GJ; Williams, SJ;
- Details
- Publication Year 2016-08-22,Volume 52,Issue #74,Page 11096-11099
- Journal Title
- Chemical Communications
- Publication Type
- Journal Article
- 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-beta-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.
- Publisher
- Royal Society Chemistry
- Research Division(s)
- Chemical Biology
- PubMed ID
- 27546776
- Publisher's Version
- https://doi.org/10.1039/c6cc04649e
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2016-09-06 09:00:25
Last Modified: 2018-07-11 09:09:22