Monte carlo simulations of enzyme reactions in two dimensions: fractal kinetics and spatial segregation.
Conventional equations for enzyme kinetics are based on mass-action laws, that may fail in low-dimensional and disordered media such as biological membranes. We present Monte Carlo simulations of an isolated Michaelis-Menten enzyme reaction on two-dimensional lattices with varying obstacle densities, as models of biological membranes. The model predicts that, as a result of anomalous diffusion on these low-dimensional media, the kinetics are of the fractal type. Consequently, the conventional equations for enzyme kinetics fail to describe the reaction. In particular, we show that the quasi-stationary-state assumption can hardly be retained in these conditions. Moreover, the fractal characteristics of the kinetics are increasingly pronounced as obstacle density and initial substrate concentration increase. The simulations indicate that these two influences are mainly additive. Finally, the simulations show pronounced S-P segregation over the lattice at obstacle densities compatible with in vivo conditions. This phenomenon could be a source of spatial self organization in biological membranes.
D001703:Biophysics / Q000379:methods*; D003198:Computer Simulation; D004058:Diffusion; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D017709:Fractals; D007700:Kinetics; D009010:Monte Carlo Method; D013997:Time Factors
D004798:Enzymes