Mechanism of catalysis by retaining beta-glycosyl hydrolases

Curr Opin Struct Biol. 1997 Oct;7(5):645-51. doi: 10.1016/s0959-440x(97)80073-5.

Abstract

Recent structural studies provide a fresh look at the catalytic mechanism of polysaccharide hydrolysis by retaining beta-glycosyl hydrolases. Highlights include insights into saccharide ring distortion, both upon binding and during the course of catalysis, and evidence for the regulation of the pKa of key catalytic residues.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Affinity Labels / chemistry
  • Affinity Labels / metabolism
  • Carbohydrate Conformation
  • Carbohydrate Metabolism*
  • Carbohydrates / chemistry*
  • Catalysis
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Epoxy Compounds / metabolism
  • Epoxy Compounds / pharmacology
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / metabolism*
  • Glycosides / chemistry
  • Glycosides / metabolism
  • Models, Molecular
  • Muramidase / chemistry
  • Protein Conformation

Substances

  • Affinity Labels
  • Carbohydrates
  • Enzyme Inhibitors
  • Epoxy Compounds
  • Glycosides
  • Glycoside Hydrolases
  • Muramidase