Nonhydrolyzable ubiquitin-isopeptide isosteres as deubiquitinating enzyme 
probes.

Shanmugham, A.; Fish, A.; Luna-Vargas, M. P. A.; Faesen, A. C.; El Oualid, F.; Sixma, T. K.; Ovaa, H.

doi:10.1021/ja101803s

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Nonhydrolyzable ubiquitin-isopeptide isosteres as deubiquitinating enzyme probes.

MPS-Authors

/persons/resource/persons208528

Faesen, A. C.
Research Group Biochemistry of Signal Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

2471739_Suppl.pdf
(Supplementary material), 619KB

Citation

Shanmugham, A., Fish, A., Luna-Vargas, M. P. A., Faesen, A. C., El Oualid, F., Sixma, T. K., et al. (2010). Nonhydrolyzable ubiquitin-isopeptide isosteres as deubiquitinating enzyme probes. Journal of the American Chemical Society, 132(26), 8834-8835. doi:10.1021/ja101803s.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-C719-1

Abstract

We demonstrate that oxime ligation is an efficient, straightforward, and generally applicable strategy for generating nonhydrolyzable ubiquitin (Ub)−isopeptide isosteres. We synthesized nonhydrolyzable K48- and K63-linked Ub−isopeptide isosteres to investigate the selectivity of deubiquitinating enzymes for specific linkages employing surface plasmon resonance spectroscopy. The results indicate that deubiquitinating enzymes specifically recognize the local peptide sequence flanking Ub-branched lysine residues in target proteins. The described strategy allows the systematic investigation of sequence requirements for substrate selectivity of deubiquitinating enzymes.