Allosteric inhibition of fructose-1,6-bisphosphatase by anilinoquinazolines.
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.
Wright
S W
SW
Pfizer Central Research, Groton, CT 06340, USA. stephen_w_wright@groton.pfizer.com
Hageman
D L
DL
McClure
L D
LD
Carlo
A A
AA
Treadway
J L
JL
Mathiowetz
A M
AM
Withka
J M
JM
Bauer
P H
PH
D000494:Allosteric Regulation / Q000187:drug effects; D000495:Allosteric Site; D000814:Aniline Compounds / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D006597:Fructose-Bisphosphatase / Q000037:antagonists & inhibitors*; D006801:Humans; D020128:Inhibitory Concentration 50; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008958:Models, Molecular; D015394:Molecular Structure; D011799:Quinazolines / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000814:Aniline Compounds; D004791:Enzyme Inhibitors; D011799:Quinazolines; D006597:Fructose-Bisphosphatase