Dynamic control of catalysis within biological cells

TL;DR

This paper introduces a dynamic enzyme catalysis theory accounting for time-dependent substrate concentrations, revealing how non-linear interactions with enzyme energy landscapes enable efficient switching between active states for cellular control.

Contribution

It presents a novel theoretical framework for enzyme catalysis in cells considering time-varying substrate levels, extending beyond traditional steady-state models.

Findings

Time-dependent substrate concentration enables enzyme state switching.

Non-linear interactions with energy landscape facilitate bifurcation.

Dynamic control of product synthesis in cells achieved.

Abstract

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.