Kinetic studies on the mechanism and regulation of rabbit liver fructose-1,6-bisphosphatase.
The interaction of Mg2+, AMP, and fructose 2,6-bisphosphate with respect to rabbit liver fructose-1,6-bisphosphatase was investigated by studying initial-rate kinetics of the system at pH 9.5. A rapid-equilibrium Random Bi Bi mechanism is suggested for the rabbit liver enzyme from the kinetic data. Our kinetic findings indicate that Mg2+ and the inhibitor AMP are mutually exclusive in their binding to fructose-1,6-bisphosphatase. This probably is the mechanism for AMP regulation of fructose-1,6-bisphosphatase and thus, to some extent, gluconeogenesis. A kinetic model for the interaction of these ligands with respect to rabbit liver fructose-1,6-bisphosphatase is presented.
Liu
F
F
Department of Biochemistry and Biophysics, Iowa State University, Ames 50011.
Fromm
H J
HJ
D000818:Animals; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D006706:Homeostasis; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008433:Mathematics; D008962:Models, Theoretical; D011817:Rabbits
D006597:Fructose-Bisphosphatase