Thermodynamic bounds on ultrasensitivity in covalent switching
arXiv:2211.10472 · doi:10.1016/j.bpj.2023.04.015
Abstract
Switch-like motifs are among the basic building blocks of biochemical networks. A common motif that can serve as an ultrasensitive switch consists of two enzymes acting antagonistically on a substrate, one making and the other removing a covalent modification. To work as a switch, such covalent modification cycles must be held out of thermodynamic equilibrium by continuous expenditure of energy. Here, we exploit the linear framework for timescale separation to establish tight bounds on the performance of any covalent-modification switch, in terms of the chemical potential difference driving the cycle. The bounds apply to arbitrary enzyme mechanisms, not just Michaelis-Menten, with arbitrary rate constants, and thereby reflect fundamental physical constraints on covalent switching.
arXiv comment29 pages, 6 figures
References in corpus (4)
- The Three Faces of the Second Law: I. Master Equation Formulation
- Stochastic thermodynamics of single enzymes and molecular motors
- Thermodynamic and Kinetic Analysis of Sensitivity Amplification in Biological Signal Transduction
- Coherence of Biochemical Oscillations is Bounded by Driving Force and Network Topology