RESUMO
Starting from a simple general reaction mechanism of activation of aspartic proteinases zymogens involving a uni- and a bimolecular simultaneous activation route and a reversible inhibition step, the time course equation of the zymogen, inhibitor and activated enzyme concentrations have been derived. Likewise, expressions for the time required for any reaction progress and the corresponding mean activation rates as well as the half-life of the global zymogen activation have been derived. An experimental design and kinetic data analysis is suggested to estimate the kinetic parameters involved in the reaction mechanism proposed.
Assuntos
Ácido Aspártico Endopeptidases/química , Inibidores Enzimáticos/química , Precursores Enzimáticos/química , Modelos Químicos , Ácido Aspártico Endopeptidases/antagonistas & inibidores , Catálise , Ativação Enzimática , Precursores Enzimáticos/antagonistas & inibidores , CinéticaRESUMO
From the kinetic study carried out in part I of this series (preceding article) an analysis quantifying the relative contribution to the global process of the uni- and bimolecular routes has been carried out. This analysis suggests a way to predict the time course of the relative contribution as well as the effect on this relative weight of the initial zymogen, inhibitor and activating enzyme concentrations.
Assuntos
Ácido Aspártico Endopeptidases/química , Inibidores Enzimáticos/química , Precursores Enzimáticos/química , Modelos Químicos , Ácido Aspártico Endopeptidases/antagonistas & inibidores , Catálise , Ativação Enzimática , Precursores Enzimáticos/antagonistas & inibidores , CinéticaRESUMO
Starting from a simple general reaction mechanism of activation of aspartic proteinase zymogens involving an uni- and a bimolecular simultaneous route, the time course equation of the concentration of the zymogen and of the activated enzyme have been derived. From these equations, an analysis quantifying the relative contribution to the global process of the two routes has been carried out for the first time. This analysis suggests a way to predict the time course of the relative contribution as well as the effect of the initial zymogen and activating enzyme concentrations, on the relative weight. An experimental design and kinetic data analysis is suggested to estimate the kinetic parameters involved in the reaction mechanism proposed. Finally, we apply some of our results to experimental data obtained by other authors in experimental studies of the activation of some aspartic proteinase zymogens.
