<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ura T</submitter><funding>Japan Society for the Promotion of Science</funding><funding>New Energy and Industrial Technology Development Organization</funding><pagination>14381</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10474089</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(1)</volume><pubmed_abstract>Biological properties of protein molecules depend on their interaction with other molecules, and enzymes are no exception. Enzyme activities are controlled by their interaction with other molecules in living cells. Enzyme activation and their catalytic properties in the presence of different types of polymers have been studied in vitro, although these studies are restricted to only a few enzymes. In this study, we show that addition of poly-l-lysine (PLL) can increase the enzymatic activity of multiple oxidoreductases through formation of enzyme assemblies. Oxidoreductases with an overall negative charge, such as l-lactate oxidase, d-lactate dehydrogenase, pyruvate oxidase, and acetaldehyde dehydrogenase, each formed assemblies with the positively charged PLL via electrostatic interactions</pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Activation of oxidoreductases by the formation of enzyme assembly.</pubmed_title><pmcid>PMC10474089</pmcid><funding_grant_id>JPNP14004</funding_grant_id><funding_grant_id>22H05437</funding_grant_id><funding_grant_id>20J21734</funding_grant_id><pubmed_authors>Shiraki K</pubmed_authors><pubmed_authors>Tamada T</pubmed_authors><pubmed_authors>Ura T</pubmed_authors><pubmed_authors>Takakusagi Y</pubmed_authors><pubmed_authors>Sakakibara N</pubmed_authors><pubmed_authors>Mikawa T</pubmed_authors><pubmed_authors>Hirano Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Activation of oxidoreductases by the formation of enzyme assembly.</name><description>Biological properties of protein molecules depend on their interaction with other molecules, and enzymes are no exception. Enzyme activities are controlled by their interaction with other molecules in living cells. Enzyme activation and their catalytic properties in the presence of different types of polymers have been studied in vitro, although these studies are restricted to only a few enzymes. In this study, we show that addition of poly-l-lysine (PLL) can increase the enzymatic activity of multiple oxidoreductases through formation of enzyme assemblies. Oxidoreductases with an overall negative charge, such as l-lactate oxidase, d-lactate dehydrogenase, pyruvate oxidase, and acetaldehyde dehydrogenase, each formed assemblies with the positively charged PLL via electrostatic interactions</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Sep</publication><modification>2025-04-25T18:41:10.529Z</modification><creation>2024-10-19T06:20:16.171Z</creation></dates><accession>S-EPMC10474089</accession><cross_references><pubmed>37658129</pubmed><doi>10.1038/s41598-023-41789-9</doi></cross_references></HashMap>