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Activation of oxidoreductases by the formation of enzyme assembly
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 o...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10474089/ https://www.ncbi.nlm.nih.gov/pubmed/37658129 http://dx.doi.org/10.1038/s41598-023-41789-9 |
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author | Ura, Tomoto Sakakibara, Nanako Hirano, Yu Tamada, Taro Takakusagi, Yoichi Shiraki, Kentaro Mikawa, Tsutomu |
author_facet | Ura, Tomoto Sakakibara, Nanako Hirano, Yu Tamada, Taro Takakusagi, Yoichi Shiraki, Kentaro Mikawa, Tsutomu |
author_sort | Ura, Tomoto |
collection | PubMed |
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. The enzyme activities of these oxidoreductases in the enzyme assemblies were several-folds higher than those of the enzyme in their natural dispersed state. In the presence of PLL, the turnover number (k(cat)) improved for all enzymes, whereas the decrease in Michaelis constant (K(M)) was enzyme dependent. This type of enzyme function regulation through the formation of assemblies via simple addition of polymers has potential for diverse applications, including various industrial and research purposes. |
format | Online Article Text |
id | pubmed-10474089 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-104740892023-09-03 Activation of oxidoreductases by the formation of enzyme assembly Ura, Tomoto Sakakibara, Nanako Hirano, Yu Tamada, Taro Takakusagi, Yoichi Shiraki, Kentaro Mikawa, Tsutomu Sci Rep Article 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. The enzyme activities of these oxidoreductases in the enzyme assemblies were several-folds higher than those of the enzyme in their natural dispersed state. In the presence of PLL, the turnover number (k(cat)) improved for all enzymes, whereas the decrease in Michaelis constant (K(M)) was enzyme dependent. This type of enzyme function regulation through the formation of assemblies via simple addition of polymers has potential for diverse applications, including various industrial and research purposes. Nature Publishing Group UK 2023-09-01 /pmc/articles/PMC10474089/ /pubmed/37658129 http://dx.doi.org/10.1038/s41598-023-41789-9 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Ura, Tomoto Sakakibara, Nanako Hirano, Yu Tamada, Taro Takakusagi, Yoichi Shiraki, Kentaro Mikawa, Tsutomu Activation of oxidoreductases by the formation of enzyme assembly |
title | Activation of oxidoreductases by the formation of enzyme assembly |
title_full | Activation of oxidoreductases by the formation of enzyme assembly |
title_fullStr | Activation of oxidoreductases by the formation of enzyme assembly |
title_full_unstemmed | Activation of oxidoreductases by the formation of enzyme assembly |
title_short | Activation of oxidoreductases by the formation of enzyme assembly |
title_sort | activation of oxidoreductases by the formation of enzyme assembly |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10474089/ https://www.ncbi.nlm.nih.gov/pubmed/37658129 http://dx.doi.org/10.1038/s41598-023-41789-9 |
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