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Computational and Mathematical Methods in Medicine
Volume 8, Issue 2, Pages 93-112
Original Article

A Study of the Temperature Dependence of Bienzyme Systems and Enzymatic Chains

1Laboratory of Biophysics and Bionics, Physics Department, Kazan State University, Kazan 420018, Russia
2Centre for Mathematical Biology, Mathematical Institute, University of Oxford, 24-29 St. Giles, Oxford OX1 3LB, UK
3Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
4Kazan Institute of Biochemistry and Biophysics, Kazan State University, Russian Academy of Sciences, Kazan 420018, Russia
5Department of Biochemistry, Oxford Centre for Integrative Systems Biology, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
6Systems Biology Lab, Department of Engineering, University of Leicester, University Road, Leicester LE1 7RH, UK

Received 6 October 2006; Revised 16 March 2007; Accepted 28 March 2007

Copyright © 2007 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


It is known that most enzyme-facilitated reactions are highly temperature dependent processes. In general, the temperature coefficient, Q10, of a simple reaction reaches 2.0–3.0. Nevertheless, some enzyme-controlled processes have much lower Q10 (about 1.0), which implies that the process is almost temperature independent, even if individual reactions involved in the process are themselves highly temperature dependent. In this work, we investigate a possible mechanism for this apparent temperature compensation: simple mathematical models are used to study how varying types of enzyme reactions are affected by temperature. We show that some bienzyme-controlled processes may be almost temperature independent if the modules involved in the reaction have similar temperature dependencies, even if individually, these modules are strongly temperature dependent. Further, we show that in non-reversible enzyme chains the stationary concentrations of metabolites are dependent only on the relationship between the temperature dependencies of the first and last modules, whilst in reversible reactions, there is a dependence on every module. Our findings suggest a mechanism by which the metabolic processes taking place within living organisms may be regulated, despite strong variation in temperature.