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.

doi:10.1039/C6CC04649E

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-0000-18B4-A

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.