[Some characteristics of the kinetics of enzymatic reactions based on the example of catalase].
A method of kinetic analysis for quickly acting enzymes, which are characterized with substrate inhibition, on the catalase model is proposed. Catalase kinetics was shown to be full described, considering changes in the maximal reaction rate and Michaelis constant, by four parameters instead of two usual ones (Vmax, Km equals const.). The method described makes possible to calculate the change the Michaelis constant in time and to estimate real dependencies of the reaction rate on time and on the substrate concentration. Moreover, the enzyme concentration and its inactivation rate at any reaction moment can be calculated under saturation conditions. It is supposed that experimental dependencies of Km on t and of Vmax on t are the results of residual conformation changes accumulated by the enzyme in the reaction process.
D002374:Catalase / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D007700:Kinetics; D008433:Mathematics; D008722:Methods; D013997:Time Factors
D002374:Catalase
O nekotorykh osobennostiakh kinetiki fermentativnykh reaktsiĭ na primere katalazy