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

Chem Commun (Camb). 2016 Sep 25;52(74):11096-9. doi: 10.1039/c6cc04649e. Epub 2016 Aug 22.

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.

MeSH terms

  • Acetylglucosamine / analogs & derivatives
  • Acetylglucosamine / chemistry
  • Acetylglucosamine / metabolism
  • Bacteroides / enzymology*
  • Binding Sites
  • Catalytic Domain
  • Crohn Disease / etiology
  • Crohn Disease / microbiology
  • Humans
  • Molecular Dynamics Simulation
  • Stereoisomerism
  • Substrate Specificity
  • Thiazoles / chemistry
  • Thiazoles / metabolism
  • beta-N-Acetyl-Galactosaminidase / chemistry
  • beta-N-Acetyl-Galactosaminidase / metabolism*

Substances

  • Thiazoles
  • 4-nitrophenyl-N-acetyl-2-deoxyglucopyranoside
  • beta-N-Acetyl-Galactosaminidase
  • Acetylglucosamine