Rohwer J.M., Hanekom A.J., Crous C., Snoep J.L., Hofmeyr J.-H.S.
Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa
Rohwer, J.M., Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa; Hanekom, A.J., Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa; Crous, C., Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa; Snoep, J.L., Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa; Hofmeyr, J.-H.S., Triple-J Group for Molecular Cell Physiology, Department of Biochemistry, Stellenbosch University, Matieland, South Africa
The evaluation of a generic simplified bi-substrate enzyme kinetic equation, whose derivation is based on the assumption of equilibrium binding of substrates and products in random order, is described. This equation is much simpler than the mechanistic (ordered and ping-pong) models, in that it contains fewer parameters (that is, no Ki values for the substrates and products). The generic equation fits data from both the ordered and the ping-pong models well over a wide range of substrate and product concentrations. In the cases where the fit is not perfect, an improved fit can be obtained by considering the rate equation for only a single set of product concentrations. Due to its relative simplicity in comparison to the mechanistic models, this equation will be useful for modelling bi-substrate reactions in computational systems biology. © The Institution of Engineering and Technology 2006.
Computational methods; Enzyme kinetics; Mathematical models; Computational systems biology; Equilibrium binding; Generic bi-substrate rate equation; Ping-pong model; Biology; article; catalysis; controlled study; enzyme binding; enzyme kinetics; enzyme mechanism; intermethod comparison; systems biology; theoretical model; Catalysis; Computational Biology; Computer Simulation; Enzyme Activation; Enzyme Inhibitors; Enzymes; Models, Biological; Models, Chemical; Models, Molecular; Substrate Specificity