The role of liquid-liquid phase separation in regulating enzyme activity

TL;DR

Liquid-liquid phase separation (LLPS) is a widespread cellular mechanism that regulates enzyme activity by altering the environment, concentrating reactants, and controlling metabolic pathways, with implications for cell survival and adaptation.

Contribution

This paper reviews recent insights into how LLPS influences enzyme catalysis, highlighting its regulatory roles and underlying mechanisms in cellular contexts.

Findings

LLPS affects the physicochemical environment of enzymes.

LLPS can concentrate reactants and modulate reaction rates.

LLPS plays a role in cell stress response and metabolic rerouting.

Abstract

Liquid-liquid phase separation is now recognized as a common mechanism for regulating enzyme activity in cells. Insights from studies in cells are complemented by in vitro studies aimed at developing better understanding of mechanisms underlying such control. These mechanisms are often based on the influence of LLPS on the physicochemical properties of the enzyme's environment. Biochemical mechanisms underlying such regulation include the potential for concentrating reactants together, tuning reaction rates, and controlling competing metabolic pathways. LLPS is thus a powerful tool with extensive utilities for the cell, e.g. for consolidating cell survival under stress or rerouting metabolic pathways in response to the energy state of the cell. By examining the evidence of how LLPS affects enzyme catalysis, we can begin to understand emerging concepts and expand our understanding of enzyme catalysis in living cells.