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

S W Wright; D L Hageman; L D McClure; A A Carlo; J L Treadway; A M Mathiowetz; J M Withka; P H Bauer

doi:10.1016/s0960-894x(00)00586-2

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.

Authors

S W Wright¹, D L Hageman, L D McClure, A A Carlo, J L Treadway, A M Mathiowetz, J M Withka, P H Bauer

Affiliation

¹ Pfizer Central Research, Groton, CT 06340, USA. stephen_w_wright@groton.pfizer.com

PMID: 11140724
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