ArticleScientific reports2023
Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid-liquid phase separation.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Citrate synthase condensation requires catalytic events in Corynebacterium glutamicum.Nature communications · 2026Article
- Activation of oxidoreductases by the formation of enzyme assembly.Scientific reports · 2023Article
- Condensate Formation by Metabolic Enzymes inMicroorganisms · 2022Review
- Protein conformation and biomolecular condensates.Current research in structural biology · 2022Review
- Enhanced deoxyviolacein bioproduction via enzyme condensation with a yeast glycolytic enzyme-derived peptide tag.Biotechnology progressArticle
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Authors and funding
8 authors.
Funding
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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
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