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Literature summary for 2.3.2.31 extracted from
- UbMES and UbFluor Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN (2017), J. Biol. Chem., 292, 16539-16553 .
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | development of chemical probes, ubiquitin C-terminal fluorescein thioesters UbMES and UbFluor, to qualitatively and quantitatively assess the activity of the RBR E3 ligase PARKIN in a simple experimental setup and in real time using fluorescence polarization. UbFluor quantitatively detects naturally occurring activation states of parkin caused by Ser65 phosphorylation and phosphorylated ubiquitin | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O60260 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | parkin does not require an E2 enzyme for substrate ubiquitination, lysine selection, and polyubiquitin chain formation. Both phosphorylated ubiquitin and the ubiquitin-accepting substrate contribute to maximal ubiquitin conjugation turnover of phosphorylated parkin. Phosphorylated ubiquitin enhances the transthiolation step, whereas the substrate clears the phosphorylated parkin-ubiquitin thioester intermediate | Homo sapiens |
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Release 2023.1 (January 2023)
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