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

Roth, C., Petricevic, M., John, A., Goddard-Borger, E. D., Davies, G. J., & Williams, S. J. (2016). Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-β-galactosaminidase that uses neighbouring group participation. Chemical Communications, 52(74), 11096-11099. doi:10.1039/C6CC04649E.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-18B4-A Version Permalink: http://hdl.handle.net/21.11116/0000-0000-18B5-9
Genre: Journal Article

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Roth, C.1, Author              
Petricevic, M., Author
John, A., Author
Goddard-Borger, E. D., Author
Davies, G. J., Author
Williams, S. J., Author
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1External Organizations, ou_persistent22              

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 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-[small 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.

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 Dates: 2016
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1039/C6CC04649E
BibTex Citekey: C6CC04649E
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Title: Chemical Communications
  Other : Chem. Commun.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 52 (74) Sequence Number: - Start / End Page: 11096 - 11099 Identifier: ISSN: 1359-7345