Kinetics of an autocatalytic zymogen reaction in the presence of an inhibitor coupled to a monitoring reaction.
A global kinetic analysis of a model consisting of an autocatalytic zymogen-activation process, in which an irreversible inhibitor competes with the zymogen for the active site of the proteinase, and a monitoring coupled reaction, in which the enzyme acts upon one of its substrates, is presented. This analysis is based on the progress curves of any of the two products released in the monitoring reaction. The general solution is applied to an important particular case in which rapid equilibrium conditions prevail. Finally, we suggest a procedure to predict whether the inhibition or activation route dominates in the steady state of the system. These results generalize our previous analysis of simpler mechanisms.
Manjabacas
M C
MC
Departamento de Química-Física, Escuela Universitaria Polítecnica deAlbacete, Universidad de Castilla-La Mancha, Spain.
Valero
E
E
García-Moreno
M
M
Garrido
C
C
Varón
R
R
D001665:Binding Sites; D002384:Catalysis; D010450:Endopeptidases / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D011480:Protease Inhibitors / Q000494:pharmacology
D004791:Enzyme Inhibitors; D004792:Enzyme Precursors; D011480:Protease Inhibitors; D010450:Endopeptidases