Kinetic analysis of a general model of activation of aspartic proteinase zymogens involving a reversible inhibitor. I. Kinetic analysis.
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.
Muñoz-López
A
A
Departamento de Química-Física, Escuela Politécnica Superior de Albacete, Universidad de Castilla-La Mancha, Albacete, Spain.
Sotos-Lomas
A
A
Arribas
E
E
Masia-Perez
J
J
Garcia-Molina
F
F
García-Moreno
M
M
Varon
R
R
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D002384:Catalysis; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000737:chemistry*; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical
D004791:Enzyme Inhibitors; D004792:Enzyme Precursors; D016282:Aspartic Acid Endopeptidases