Dynamic control of catalysis within biological cells

We develop a theory of enzyme catalysis within biological cells where the substrate concentration [S](t) is time dependent, in contrast to the Michaelis-Menten theory that assumes a steady state. We find that the time varying concentration can combine, in a non-linear way, with the ruggedness of the free energy landscape of enzymes (discovered both in single molecule studies and in simulations) to provide a highly efficient switch (or, bifurcation) between two catalytically active states, at a critical substrate concentration. This allows a dynamic control of product synthesis in cell.

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