Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid-liquid phase separation.

ABSTRACT: The assembly state of enzymes is gaining interest as a mechanism for regulating the function of enzymes in living cells. One of the current topics in enzymology is the relationship between enzyme activity and the assembly state due to liquid-liquid phase separation. In this study, we demonstrated enzyme activation via the formation of enzyme assemblies using L-lactate oxidase (LOX). LOX formed hundreds of nanometer-scale assemblies with poly-L-lysine (PLL). In the presence of ammonium sulfate, the LOX-PLL clusters formed micrometer-scale liquid droplets. The enzyme activities of LOX in clusters and droplets were one order of magnitude higher than those in the dispersed state, owing to a decrease in K_M and an increase in k_cat. Moreover, the clusters exhibited a higher

SUBMITTER: Ura T 

PROVIDER: S-EPMC9877012 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature