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Literature summary for 2.7.11.15 extracted from

  • Touhara, K.
    Binding of multiple ligands to pleckstrin homology domain regulates membrane translocation and enzyme activity of beta-adrenergic receptor kinase (1997), FEBS Lett., 417, 243-248.
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
beta-ARK expression in SF9 cells Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
peptide synthetic peptides derived from the receptor intracellular loop inhibit Bos taurus

Localization

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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant beta-ARK expressed in Sf9 cells Bos taurus

Substrates and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Bos taurus