Glycoside hydrolases: catalytic base/nucleophile diversity

Biotechnol Bioeng. 2010 Oct 1;107(2):195-205. doi: 10.1002/bit.22838.

Abstract

Recent studies have shown that a number of glycoside hydrolase families do not follow the classical catalytic mechanisms, as they lack a typical catalytic base/nucleophile. A variety of mechanisms are used to replace this function, including substrate-assisted catalysis, a network of several residues, and the use of non-carboxylate residues or exogenous nucleophiles. Removal of the catalytic base/nucleophile by mutation can have a profound impact on substrate specificity, producing enzymes with completely new functions.

Publication types

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

MeSH terms

  • Bacteria / enzymology*
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism*
  • Humans
  • Models, Chemical
  • Models, Molecular
  • Protein Structure, Tertiary
  • Substrate Specificity

Substances

  • Glycoside Hydrolases