Allosteric inhibition of fructose-1,6-bisphosphatase by anilinoquinazolines

Bioorg Med Chem Lett. 2001 Jan 8;11(1):17-21. doi: 10.1016/s0960-894x(00)00586-2.

Abstract

Anilinoquinazolines currently of interest as inhibitors of tyrosine kinases have been found to be allosteric inhibitors of the enzyme fructose 1,6-bisphosphatase. These represent a new approach to inhibition of F16BPase and serve as leads for further drug design. Enzyme inhibition is achieved by binding at an unidentified allosteric site.

MeSH terms

  • Allosteric Regulation / drug effects
  • Allosteric Site
  • Aniline Compounds / chemical synthesis
  • Aniline Compounds / chemistry
  • Aniline Compounds / pharmacology*
  • Animals
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Fructose-Bisphosphatase / antagonists & inhibitors*
  • Humans
  • Inhibitory Concentration 50
  • Kidney / enzymology
  • Liver / enzymology
  • Models, Molecular
  • Molecular Structure
  • Quinazolines / chemical synthesis
  • Quinazolines / chemistry
  • Quinazolines / pharmacology*
  • Structure-Activity Relationship

Substances

  • Aniline Compounds
  • Enzyme Inhibitors
  • Quinazolines
  • Fructose-Bisphosphatase