title: The allosteric properties of beef-liver fructose bisphosphatase.
abstract: 1. The activity of beef liver fructose bisphosphatase has been shown to respond cooperatively to increasing concentrations of the activating cations Mg2+ and Mn2+. The allosteric inhibitor AMP caused an increase in this cooperativity and a decrease in the apparent affinity of the enzyme for the activating cation. 2. The cooperative response of the enzyme to AMP is similarly increased by increasing cation concentrations with a concomitant decrease in the apparent affinity. 3. Direct binding experiments indicated that in the absence of either Mg2+ or Mn2+ the enzyme bound AMP non-cooperatively up to a maximum of two molecules per molecule of enzyme, a result that is indicative of half-sites reactivity. The binding became increasingly cooperative as the concentration of the activating cation was increased. 4. The substrate fructose bisphosphate had no effect on any of these cooperative responses. 5. These results may be most simply interpreted in terms of concerted model in which the activating cation functions both as an allosteric activator and as an essential cofactor for the reaction.
mesh_terms: D000249:Adenosine Monophosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000495:Allosteric Site; D004492:Edetic Acid / Q000494:pharmacology; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005636:Fructosephosphates / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008433:Mathematics; D008954:Models, Biological; D011485:Protein Binding
chemical_list: D005636:Fructosephosphates; D000249:Adenosine Monophosphate; D008345:Manganese; D004492:Edetic Acid; D006597:Fructose-Bisphosphatase; D008274:Magnesium