Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion

Cells compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here, the authors describe a self-assembly approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability, and observe an inversed correlation between the protein size and the activity enh...

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Autores principales: Zhao Zhao, Jinglin Fu, Soma Dhakal, Alexander Johnson-Buck, Minghui Liu, Ting Zhang, Neal W. Woodbury, Yan Liu, Nils G. Walter, Hao Yan
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/0c8994d2379840b6bc7c9a797d47c2d7
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spelling oai:doaj.org-article:0c8994d2379840b6bc7c9a797d47c2d72021-12-02T14:40:15ZNanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion10.1038/ncomms106192041-1723https://doaj.org/article/0c8994d2379840b6bc7c9a797d47c2d72016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10619https://doaj.org/toc/2041-1723Cells compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here, the authors describe a self-assembly approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability, and observe an inversed correlation between the protein size and the activity enhancement.Zhao ZhaoJinglin FuSoma DhakalAlexander Johnson-BuckMinghui LiuTing ZhangNeal W. WoodburyYan LiuNils G. WalterHao YanNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Zhao Zhao
Jinglin Fu
Soma Dhakal
Alexander Johnson-Buck
Minghui Liu
Ting Zhang
Neal W. Woodbury
Yan Liu
Nils G. Walter
Hao Yan
Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
description Cells compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here, the authors describe a self-assembly approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability, and observe an inversed correlation between the protein size and the activity enhancement.
format article
author Zhao Zhao
Jinglin Fu
Soma Dhakal
Alexander Johnson-Buck
Minghui Liu
Ting Zhang
Neal W. Woodbury
Yan Liu
Nils G. Walter
Hao Yan
author_facet Zhao Zhao
Jinglin Fu
Soma Dhakal
Alexander Johnson-Buck
Minghui Liu
Ting Zhang
Neal W. Woodbury
Yan Liu
Nils G. Walter
Hao Yan
author_sort Zhao Zhao
title Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
title_short Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
title_full Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
title_fullStr Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
title_full_unstemmed Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
title_sort nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/0c8994d2379840b6bc7c9a797d47c2d7
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AT yanliu nanocagedenzymeswithenhancedcatalyticactivityandincreasedstabilityagainstproteasedigestion
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