![]() |
|
|
Molecular Pharmacology, Vol 3, 177-187, Copyright © 1967 by the American Society for Pharmacology and Experimental Therapeutics
1 Department of Pharmacology, Stanford University School of Medicine,
Palo Alto, California 94304
This paper describes the kinetics of phosphofructokinase from the liver fluke Fasciola hepatica. Activation of the enzyme was accompanied by a marked increase in its affinity for both fructose-6-P and ATP. Results with the activated enzyme showed that each of the three ligands (fructose-6-P, ATP and cyclic 3',5'-AMP) could alter the saturation function of the other. The enzyme was strongly inhibited by ATP in the presence of low fructose-6-P concentrations. Both cyclic 3',5'-AMP and fructose-6-P could increase the concentrations of ATP required to produce 50% inhibition. Possible interaction among the substrates and the effector ligands on the enzyme was considered in terms of the Monod-Changeux-Wyman model for allosteric proteins. Saturation curves for fructose-6-P indicated cooperative homotropic interactions between multiple binding sites for this substrate. ATP at high concentration increased the homotropic interactions while cyclic 3',5'-AMP had the opposite effect. The saturation function of cyclic 3',5'-AMP was also shown to be influenced by both enzyme substrates. Fructose-6-P at high concentration caused a decrease in the half-saturation point for cyclic 3',5'-AMP while ATP had the opposite effect. Saturation curves for Mg++ were also altered by a change in concentration of fructose-6-P, ATP or cyclic 3',5'-AMP. The possible role of these kinetic properties on the fine regulation of activated phosphofructokinase was discussed.
Note:
ACKNOWLEDGMENTS
This work was supported by Research Grant
AI04214 from the National Institute of Allergy
and Infectious Diseases, U. S. Public Health
Service; and a Research Career Development
Award GM-K3-3848 from the Division of General Medical Sciences, U. S. Public Health Service.
This article has been cited by other articles:
![]() |
T. Mansour Chemotherapy of parasitic worms: new biochemical strategies Science, August 3, 1979; 205(4405): 462 - 469. [Abstract] [PDF] |
||||