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

TY - JOUR

T1 - Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-β-galactosaminidase that uses neighbouring group participation

AU - Roth, C.

AU - Petricevic, M.

AU - John, A.

AU - Goddard-Borger, E. D.

AU - Davies, G. J.

AU - Williams, S. J.

N1 - ©The Royal Society of Chemistry 2016.

PY - 2016/9/25

Y1 - 2016/9/25

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84987638045&partnerID=8YFLogxK

U2 - 10.1039/c6cc04649e

DO - 10.1039/c6cc04649e

M3 - Article

AN - SCOPUS:84987638045

VL - 52

SP - 11096

EP - 11099

JO - Chemical communications

JF - Chemical communications

SN - 1359-7345

IS - 74

ER -