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

DOI: 10.1039/C6CC04649E DOI Help

Authors: C. Roth (Department of Chemistry, University of York, Diamond Light Source) , M. Petricevic (School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne) , A. John (ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research; Department of Medical Biology, University of Melbourne) , E. D. Goddard-borger (ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research; Department of Medical Biology, University of Melbourne) , G. J. Davies (Department of Chemistry, University of York, Diamond Light Source) , S. J. Williams (School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chem. Commun.

State: Published (Approved)
Published: August 2016
Diamond Proposal Number(s): 9948

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-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.

Subject Areas: Biology and Bio-materials, Medicine, Chemistry


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 26/08/2016 14:47

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