A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine

Org Biomol Chem. 2011 Sep 7;9(17):5945-7. doi: 10.1039/c1ob05766a. Epub 2011 Jul 25.

Abstract

Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site.

MeSH terms

  • Alicyclobacillus / enzymology*
  • Cellulase / antagonists & inhibitors*
  • Cellulase / metabolism
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Glycoside Hydrolases
  • Imino Pyranoses / chemistry*
  • Imino Pyranoses / pharmacology*
  • Models, Molecular
  • Protein Binding

Substances

  • Enzyme Inhibitors
  • Imino Pyranoses
  • isofagomine
  • Glycoside Hydrolases
  • Cellulase