The monovalent cation-induced association of formyltetrahydrofolate synthetase subunits. Kinetic and thermodynamic aspects.
Formyltetrahydrofolate synthetase monomers are converted to catalytically active tetramers in the presence of monovalent cations. The stoichiometry of the reaction is 4M + 2C+ in equilibrium M4C2(2+). A positive deltaS compensates for an unfavorable positive deltaH so that the overall reaction is exergonic. Both deltaH and deltaS become more positive as the temperature is increased. Association of subunits of the enzyme prepared from Clostridium cylindrosporum is second order with respect to monomer concentration, consistent with a rate-determining dimerization step. Activation parameters for this step at 20 degrees are: deltaG, 12.6 kcal mol-1; deltaH, 12.5 kcal mol-1; deltaS, -05 e.u. The rate-limiting step for the cation-dependent association of Clostridium acidi-urici monomers is believed to be a conformational alteration since first order kinetics is observed. The Eyring plot of the kinetic data obtained for the C. acidi-urici system has a sharp break at 15 degrees. Activation parameters for cation-induced association at 20 degrees are: deltaG, 21.5 kcal  mol-1; deltaH, 14.0 kcal mol-1; deltaS, -26.6 e.u.
D001665:Binding Sites; D002151:Calorimetry; D002414:Cations, Monovalent; D003013:Clostridium / Q000201:enzymology; D005574:Formate-Tetrahydrofolate Ligase / Q000378:metabolism*; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
D002414:Cations, Monovalent; D046911:Macromolecular Substances; D008025:Ligases; D005574:Formate-Tetrahydrofolate Ligase