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Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades

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Varón R., Havsteen B. H., Valero E., Molina-Alarcón M., García-Cánovas F., García-Moreno M.

2005

vol. 52

issue 4

765-780

This paper presents a kinetic analysis of the whole reaction course, i.e. of both the transient phase and the steady state, of open multicyclic enzyme cascade systems. Equations for fractional modifications are obtained which are valid for the whole reaction course. The steady state expressions for the fractional modifications were derived from the latter equations since they are not restricted to the condition of rapid equilibrium. Finally, the validity of our results is discussed and tested by numerical integration. Apart from the intrinsic value of knowing the kinetic behaviour of any of the species involved in any open multicyclic enzyme cascade, the kinetic analysis presented here can be the basis of future contributions concerning open multicyclic enzyme cascades which require the knowledge of their time course equations (e.g. evaluation of the time needed to reach the steady state, suggestion of kinetic data analysis, etc.), analogous to those already carried out for open bicyclic cascades.

Contribution of the intra- and intermolecular routes in autocatalytic zymogen activation: application to pepsinogen activation

100%

Varón R., Fuentes M. E., García-Moreno M., Garcìa-Sevilla F., Arias E., Valero E., Arribas E.

2006

vol. 53

issue 2

407-420

Taking as the starting point a recently suggested reaction scheme for zymogen activation involving intra- and intermolecular routes and the enzyme-zymogen complex, we carry out a complete analysis of the relative contribution of both routes in the process. This analysis suggests the definition of new dimensionless parameters allowing the elaboration, from the values of the rate constants and initial conditions, of the time course of the contribution of the two routes. The procedure mentioned above related to a concrete reaction scheme is extrapolated to any other model of autocatalytic zymogen activation involving intra- and intermolecular routes. Finally, we discuss the contribution of both of the activating routes in pepsinogen activation into pepsin using the values of the kinetic parameters given in the literature.

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2 Acta Biochimica Polonica

1 2006

1 2005

2 García-Moreno M.

2 Valero E.

2 Varón R.

1 Arias E.

1 Arribas E.

1 Fuentes M. E.

1 Garcìa-Sevilla F.

1 García-Cánovas F.

1 Havsteen B. H.

1 Molina-Alarcón M.

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Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades

Contribution of the intra- and intermolecular routes in autocatalytic zymogen activation: application to pepsinogen activation