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Literature summary for 2.7.1.1 extracted from
- Allosteric activation of human glucokinase by free polyubiquitin chains and its ubiquitin-dependent cotranslational proteasomal degradation (2007), J. Biol. Chem., 282, 22757-22764.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| pentaubiquitin | the recombinant glucokinase is allosterically activated up to 1.4fold by purified free pentaubiquitin chains at about 100 nM, and possibly also by unidentified polyubiquitinated proteins | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | poly/multiubiquitination of glucokinase in vitro serves as a signal for proteasomal degradation of the newly synthesized protein | Homo sapiens |
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