A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases

FEBS Lett. 2003 Mar 13;538(1-3):1-7. doi: 10.1016/s0014-5793(03)00148-0.

Abstract

An in silico survey of the -1 subsite of all known 3D-structures of O-glycoside hydrolases containing a suitably positioned ligand has led to the recognition -- apparently without exceptions -- of a transition state stabilising hydrophobic platform which is complementary to a crucial hydrophobic patch of the ligand. This platform is family-specific and highly conserved. A comprehensive list is given with examples of enzymes belonging to 33 different families. Several typical constellations of platform - protein residues are described.

Publication types

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

MeSH terms

  • Animals
  • Binding Sites
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / metabolism*
  • Species Specificity

Substances

  • Glycoside Hydrolases