The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases
Open accessAbstract
Active-site directed probes are powerful in studies of enzymatic function. We report an active-site directed probe based on a warhead so far considered unreactive. By replacing the C-terminal carboxylate of ubiquitin (Ub) with an alkyne functionality, a selective reaction with the active-site cysteine residue of de-ubiquitinating enzymes was observed. The resulting product was shown to be a quaternary vinyl thioether, as determined by X-ray crystallography. Proteomic analysis of proteins bound to an immobilized Ub alkyne probe confirmed the selectivity toward de-ubiquitinating enzymes. The observed reactivity is not just restricted to propargylated Ub, as highlighted by the selective reaction between caspase-1 (interleukin converting enzyme) and a propargylated peptide derived from IL-1β, a caspase-1 substrate.
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Metadata
- Authors
- Ekkebus, R., van Kasteren, S. I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P. P., de Jong, A., Goerdayal, S., Neefjes, J., Heck, A. J. R., Komander, D., & Ovaa, H.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-02-15
- Volume
- 135
- Issue
- 8
- Pages
- 2867-2870
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2099598643
- Cited by
- 347
- References
- 25
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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