Beta-adrenergic-receptor kinase
In enzymology, a beta-adrenergic-receptor kinase (EC 2.7.11.15) is an enzyme that catalyzes the chemical reaction:
- ATP + [beta-adrenergic receptor] ADP + phospho-[beta-adrenergic receptor]
| beta-adrenergic receptor kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.11.15 | ||||||||
| CAS no. | 102925-39-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are ATP and beta-adrenergic receptor, whereas its two products are ADP and phospho-beta-adrenergic receptor.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[beta-adrenergic receptor] phosphotransferase. Other names in common use include ATP:beta-adrenergic-receptor phosphotransferase, [beta-adrenergic-receptor] kinase, beta-adrenergic receptor-specific kinase, beta-AR kinase, beta-ARK, beta-ARK 1, beta-ARK 2, beta-receptor kinase, GRK2, GRK3, beta-adrenergic-receptor kinase (phosphorylating), beta2ARK, betaARK1, beta-adrenoceptor kinase, beta-adrenoceptor kinase 1, beta-adrenoceptor kinase 2, ADRBK1, BARK1, adrenergic receptor kinase, and STK15. Several compounds are known to inhibit this enzyme, including Zinc, and Digitonin.
References
- Benovic JL, Mayor F Jr, Staniszewski C, Lefkowitz RJ, Caron MG (1987). "Purification and characterization of the beta-adrenergic receptor kinase". J. Biol. Chem. 262 (19): 9026–32. doi:10.1016/S0021-9258(18)48041-6. PMID 3036840.
- Kim CM, Dion SB, Onorato JJ, Benovic JL (1993). "Expression and characterization of two beta-adrenergic receptor kinase isoforms using the baculovirus expression system". Receptor. 3 (1): 39–55. PMID 8394172.
- A, Ungerer M; Kronsbein, K; Schmitt, M; Hoffmann, K; Seyfarth, M; Schömig, A; Ungerer, M (1997). "Characterization and inhibition of beta-adrenergic receptor kinase in intact myocytes". Cardiovasc. Res. 35 (2): 324–33. doi:10.1016/S0008-6363(97)00102-8. PMID 9349395.
- Ferguson SS, Menard L, Barak LS, Koch WJ, Colapietro AM, Caron MG (1995). "Role of phosphorylation in agonist-promoted beta 2-adrenergic receptor sequestration. Rescue of a sequestration-defective mutant receptor by beta ARK1". J. Biol. Chem. 270 (42): 24782–9. doi:10.1074/jbc.270.42.24782. PMID 7559596.
- Willets JM, Challiss RA, Nahorski SR (2003). "Non-visual GRKs: are we seeing the whole picture?". Trends Pharmacol. Sci. 24 (12): 626–33. doi:10.1016/j.tips.2003.10.003. PMID 14654303.
