Kinetic analysis of a general model of activation of aspartic proteinase zymogens involving a reversible inhibitor. II. Contribution of the uni- and bimolecular activation routes.
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.
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
Escribano
J
J
Masia-Perez
J
J
Muñoz-Muñoz
J L
JL
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