Structural highlights
Publication Abstract from PubMed
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.
Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-beta-galactosaminidase that uses neighbouring group participation.,Roth C, Petricevic M, John A, Goddard-Borger ED, Davies GJ, Williams SJ Chem Commun (Camb). 2016 Sep 25;52(74):11096-9. doi: 10.1039/c6cc04649e. Epub, 2016 Aug 22. PMID:27546776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roth C, Petricevic M, John A, Goddard-Borger ED, Davies GJ, Williams SJ. Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-beta-galactosaminidase that uses neighbouring group participation. Chem Commun (Camb). 2016 Sep 25;52(74):11096-9. doi: 10.1039/c6cc04649e. Epub, 2016 Aug 22. PMID:27546776 doi:http://dx.doi.org/10.1039/c6cc04649e
