Kinetics of enzyme systems with unstable suicide substrates.

This paper deals with kinetic studies of enzyme reaction mechanisms with enzyme inactivation induced by an unstable suicide substrate. An initial steady-state of the catalytic route is assumed and the time course equations for the total active enzyme forms and the reaction product have been derived. The goodness of the analytical solutions has been tested by comparison with the simulated curves obtained by numerical integration. A kinetic data analysis to determine the corresponding kinetic parameters is suggested and the time course equations of an important reaction mechanisms involving a stable suicide substrate and which can be regarded as particular case of that under study has also been derived from the corresponding equations. The simplicity of our method allows its systematic application to more complex mechanisms.