Enzymatic metabolons dramatically enhance metabolic fluxes of low-efficiency biochemical reactions.

ABSTRACT: In this work, we investigate how spatial proximity of enzymes belonging to the same pathway (metabolon) affects metabolic flux. Using off-lattice Langevin dynamics simulations in tandem with a stochastic reaction-diffusion protocol and a semi-analytical reaction-diffusion model, we systematically explored how strength of protein-protein interactions, catalytic efficiency, and protein-ligand interactions affect metabolic flux through the metabolon. Formation of a metabolon leads to a greater speedup for longer pathways and especially for reaction-limited enzymes, whereas, for fully optimized diffusion-limited enzymes, the effect is negligible. Notably, specific cluster architectures are not a prerequisite for enhancing reaction flux. Simulations uncover the crucial role of optimal nonspecif

SUBMITTER: Ranganathan S 

PROVIDER: S-EPMC10719048 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature