Escherichia coli succinic thiolinase. Stoichiometry of phosphorylation and coenzyme A binding.

摘要: Equilibrium and covalent binding studies of succinic thiokinase from Escherichia coli indicates that there can be a stoichiometric relationship between coenzyme A the phosphoyrlation capacity enzyme. comparison homogeneous enzyme preparations has revealed high specific activity exhibits greater this property is proportional to activity. Phosphorylation was related in highly active preparations, but leveled off at 1 mol phosphorus/mol thiokinase. These show "dimer dimers" structure contains expected two sites does not demonstrate "half-the-sites" reactivity. site lower affinity detected some samples Binding higher may involve positive cooperativity. ATP, unlike ADP, bind phosphorylated