Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades.
Author(s) -
R. Varón,
B. Havsteen,
Edelmira Valero,
Milagros MolinaAlarcón,
Francisco Garcı́a-Cánovas,
M. Garcı́a-Moreno
Publication year - 2005
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2005_3388
Subject(s) - cascade , kinetic energy , steady state (chemistry) , transient (computer programming) , chemistry , enzyme kinetics , thermodynamics , statistical physics , enzyme , physics , classical mechanics , computer science , chromatography , active site , biochemistry , operating system
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.
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