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
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
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
de Jong, Annemieke
Witting, Katharina
Kooij, Raymond
Flierman, Dennis
Ovaa, Huib

DOI
10.1002/anie.201706738
URN
urn:nbn:de:101:1-2022091208320417421461
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:23 AM CEST

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Associated

  • de Jong, Annemieke
  • Witting, Katharina
  • Kooij, Raymond
  • Flierman, Dennis
  • Ovaa, Huib

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