Acta Biochim Pol. 2005;52(4):765-80. Epub 2005 Aug 05.

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

Acta biochimica Polonica

Ramón Varón, Bent H Havsteen, Edelmira Valero, Milagros Molina-Alarcón, Francisco García-Cánovas, Manuela García-Moreno

PMID: 16086076

Abstract

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.

Substances

• Enzymes

MeSH terms

• Computer Simulation
• Enzymes / metabolism
• Kinetics
• Models, Theoretical
• Reproducibility of Results

Publication Types

• Journal Article
• Research Support, Non-U.S. Gov't
• Review