Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry

Authors :: Mason, Daniel E.
Ek, Jared
Peters, Eric C.
Harris, Jennifer L.
Neels, Jaap G.
Churchill, Michael J.
Dawson, Philip
Oldziej, Stanislaw
Jagielska, Anna;
Source :: Biochemistry. June 1, 2004, Vol. 43 Issue 21, p6535, 9 p.
Publication Year :: 2004
Abstract: Deconjugation of ubiquitin from cellular proteins is catalyzed by the deubiquitin hydrolase (DUB) family of enzymes and is an important component of the ubiquitin regulatory system affecting cellular function beyond maintenance of monomeric pools of ubiquitin. UCH-L3 efficiently cleaves small C-terminal amides of ubiquitin.

Subjects :: Protein metabolism -- Observations
Cellular proteins -- Research
Cellular proteins -- Chemical properties
Ubiquitin -- Research
Ubiquitin -- Chemical properties
Biological sciences
Chemistry

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