Release of Enzymatically Active Deubiquitinating Enzymes upon Reversible Capture by Disulfide Ubiquitin Reagents
Abstract: Deubiquitinating enzymes (DUBs) catalyze the cleavage of ubiquitin from target proteins. Ubiquitin is post‐translationally attached to proteins and serves as an important regulatory signal for key cellular processes. In this study, novel activity‐based probes to study DUBs were synthesized that comprise a ubiquitin moiety and a novel disulfide warhead at the C‐terminus. These reagents can bind DUBs covalently by forming a disulfide bridge between the active‐site cysteine residue and the ubiquitin‐based probe. As disulfide bridges can be broken by the addition of a reducing agent, these novel ubiquitin reagents can be used to capture and subsequently release catalytically active DUBs, whereas existing capturing agents bind irreversibly. These novel reagents allow for the study of these enzymes in their active state under various conditions.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Release of Enzymatically Active Deubiquitinating Enzymes upon Reversible Capture by Disulfide Ubiquitin Reagents ; volume:56 ; number:42 ; year:2017 ; pages:12967-12970 ; extent:4
Angewandte Chemie / International edition. International edition ; 56, Heft 42 (2017), 12967-12970 (gesamt 4)
- Creator
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de Jong, Annemieke
Witting, Katharina
Kooij, Raymond
Flierman, Dennis
Ovaa, Huib
- DOI
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10.1002/anie.201706738
- URN
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urn:nbn:de:101:1-2022091208320417421461
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:23 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- de Jong, Annemieke
- Witting, Katharina
- Kooij, Raymond
- Flierman, Dennis
- Ovaa, Huib