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Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes.

ABSTRACT: We report a new class of deubiquitinating enzyme (DUB) probes that resemble the native diubiquitin with a same linkage size and contain a Michael addition acceptor for trapping the DUB active-site cysteine. Both K63- and K48-linked diubiquitin probes were generated using a facile chemical ligation method. The diUb probes were demonstrated to label DUBs from different families and revealed intrinsic linkage specificities of DUBs.

SUBMITTER: Li G

PROVIDER: S-EPMC3918478 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes.

Li Guorui G Liang Qin Q Gong Ping P Tencer Adam H AH Zhuang Zhihao Z

Chemical communications (Cambridge, England) 20140101 2

We report a new class of deubiquitinating enzyme (DUB) probes that resemble the native diubiquitin with a same linkage size and contain a Michael addition acceptor for trapping the DUB active-site cysteine. Both K63- and K48-linked diubiquitin probes were generated using a facile chemical ligation method. The diUb probes were demonstrated to label DUBs from different families and revealed intrinsic linkage specificities of DUBs. ...[more]

PMID: 24225431

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