Activation of oxidoreductases by the formation of enzyme assembly.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
01 09 2023
Historique:
received: 03 07 2023
accepted: 31 08 2023
medline: 4 9 2023
pubmed: 2 9 2023
entrez: 1 9 2023
Statut: epublish

Résumé

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

Identifiants

pubmed: 37658129
doi: 10.1038/s41598-023-41789-9
pii: 10.1038/s41598-023-41789-9
pmc: PMC10474089
doi:

Substances chimiques

L-Lactate Dehydrogenase EC 1.1.1.27
Lysine K3Z4F929H6
Poly A 24937-83-5
Polymers 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

14381

Informations de copyright

© 2023. Springer Nature Limited.

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Auteurs

Tomoto Ura (T)

Institute for Quantum Life Science, National Institutes for Quantum Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, Japan.
Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573, Japan.
RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.

Nanako Sakakibara (N)

Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573, Japan.
RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.

Yu Hirano (Y)

Institute for Quantum Life Science, National Institutes for Quantum Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, Japan.
Department of Quantum Life Science, Graduate School of Science, Chiba University, Yayoi-cho, Inage-ku, Chiba, 263-8522, Japan.

Taro Tamada (T)

Institute for Quantum Life Science, National Institutes for Quantum Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, Japan.
Department of Quantum Life Science, Graduate School of Science, Chiba University, Yayoi-cho, Inage-ku, Chiba, 263-8522, Japan.

Yoichi Takakusagi (Y)

Institute for Quantum Life Science, National Institutes for Quantum Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, Japan.
Department of Quantum Life Science, Graduate School of Science, Chiba University, Yayoi-cho, Inage-ku, Chiba, 263-8522, Japan.

Kentaro Shiraki (K)

Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573, Japan.

Tsutomu Mikawa (T)

RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan. mikawa@riken.jp.

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Classifications MeSH