Distortion of mannoimidazole supports a B2,5 boat transition state for the family GH125 α-1,6-mannosidase from Clostridium perfringens

Org Biomol Chem. 2019 Aug 28;17(34):7863-7869. doi: 10.1039/c9ob01161g.

Abstract

Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 α-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Catalytic Domain
  • Clostridium perfringens / enzymology*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism*
  • Imidazoles / chemistry
  • Imidazoles / metabolism*
  • Mannose / analogs & derivatives
  • Mannose / metabolism*
  • Molecular Conformation
  • Mutation
  • Protein Binding
  • alpha-Mannosidase / chemistry
  • alpha-Mannosidase / genetics
  • alpha-Mannosidase / metabolism*

Substances

  • Enzyme Inhibitors
  • Imidazoles
  • alpha-Mannosidase
  • Mannose