Author:
Ura Tomoto,Kagawa Ako,Sakakibara Nanako,Yagi Hiromasa,Tochio Naoya,Kigawa Takanori,Shiraki Kentaro,Mikawa Tsutomu
Abstract
AbstractThe 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 inKMand an increase inkcat. Moreover, the clusters exhibited a higher activation effect than the droplets. In addition, the conformation of LOX changed in the clusters, resulting in increased enzyme activation. Understanding enzyme activation and assembly states provides important information regarding enzyme function in living cells, in addition to biotechnology applications.
Funder
JSPS Fellows
Leave a Nest grant Fundamental Biotechnology award
Japan Society for the Promotion of Science
New Energy and Industrial Technology Development Organization
Publisher
Springer Science and Business Media LLC
Cited by
3 articles.
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