Activating Compound | Comment | Organism | Structure |
---|---|---|---|
G protein betagamma-subunit | requirement, binding plays an important role in specifically targeting the enzyme complex to its receptor substrate | Bos taurus |
Cloned (Comment) | Organism |
---|---|
beta-ARK expression in SF9 cells | Bos taurus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
peptide | synthetic peptides derived from the receptor intracellular loop inhibit | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the PH domain ligands betagamma subunits of G proteins and phosphatidylinositol 4,5-bisphosphate affect membrane localization of enzyme, simultaneous presence of both ligands is required for effective membrane localization, cooperative binding of the ligands, membrane translocation | Bos taurus | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant beta-ARK expressed in Sf9 cells | Bos taurus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + beta-adrenergic receptor | specifically phosphorylates the agonist-occupied form of the receptor | Bos taurus | ADP + phospho-beta-adrenergic receptor | - |
? | |
additional information | role of the PH domain, ligand binding characteristics of the PH domain, distinct role for each ligand, i.e. betagamma subunits of G proteins and phosphatidylinositol 4,5-bisphosphate, in enzyme-mediated receptor phosphorylation | Bos taurus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Bos taurus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bos taurus |