Approaches to labeling and identification of active site residues in glycosidases

Protein Sci. 1995 Mar;4(3):361-72. doi: 10.1002/pro.5560040302.

Abstract

Glycosidases play a key role in a number of biological processes and, as such, are of considerable clinical and biotechnological importance. Knowledge of the identifies of catalytically important active site residues is essential for understanding the catalytic mechanism, for enzyme classification, and for targeted bioengineering of glycosidases with altered characteristics. Here we review and discuss traditional strategies and novel approaches based on tandem mass spectrometry for the identification of the key active site residues in glycosidases.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites*
  • Catalysis
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / metabolism*
  • Mass Spectrometry
  • Models, Chemical
  • Molecular Probes
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment

Substances

  • Molecular Probes
  • Glycoside Hydrolases