Studies on the mechanism of action of the histone kinase dependent on adenosine 3',5'-monophosphate. Fast kinetics of histone H1 phosphorylation.
The transient phase of histone H1 phosphorylation was studied by the quenched-flow method. A 'minimal' kinetic scheme of the above process was proposed. A formal kinetic analysis was given to a four-step mechanism of the reaction. Computer simulation of the transient-phase kinetics of H1 phosphorylation and the steady-state kinetics of phosphate transfer from the enzyme phosphoform to histone permitted us to estimate all kinetic constants of the proposed mechanism.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002384:Catalysis; D000242:Cyclic AMP / Q000502:physiology*; D006657:Histones / Q000302:isolation & purification; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D010766:Phosphorylation; D006656:Protamine Kinase / Q000502:physiology*; D011494:Protein Kinases / Q000502:physiology*; D013552:Swine
D006657:Histones; C025301:histone H1 phosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase