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| Name = beta-adrenergic receptor kinase
| EC_number = 2.7.11.15
| CAS_number = 102925-39-3
| IUBMB_EC_number = 2/7/11/15
| GO_code = 0047696
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In enzymology, a beta-adrenergic-receptor kinase ({{EC number|2.7.11.15}}) is an enzyme that catalyzes the chemical reaction:
ATP + [beta-adrenergic receptor]ADP + phospho-[beta-adrenergic receptor]
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
- {{cite journal | vauthors = Benovic JL, ((Mayor F Jr)), Staniszewski C, Lefkowitz RJ, Caron MG | year = 1987 | title = Purification and characterization of the beta-adrenergic receptor kinase | journal = J. Biol. Chem. | volume = 262 | issue = 19 | pages = 9026–32 | pmid = 3036840 }}
- {{cite journal | vauthors = Kim CM, Dion SB, Onorato JJ, Benovic JL | year = 1993 | title = Expression and characterization of two beta-adrenergic receptor kinase isoforms using the baculovirus expression system | journal = Receptor. | volume = 3 | pages = 39–55 | pmid = 8394172 | issue = 1 }}
- {{cite journal | author = A, Ungerer M | year = 1997 | title = Characterization and inhibition of beta-adrenergic receptor kinase in intact myocytes | journal = Cardiovasc. Res. | volume = 35 | pages = 324–33 | pmid = 9349395 | doi = 10.1016/S0008-6363(97)00102-8 | last2 = Kronsbein | first2 = K | last3 = Schmitt | first3 = M | last4 = Hoffmann | first4 = K | last5 = Seyfarth | first5 = M | last6 = Schömig | first6 = A | last7 = Ungerer | first7 = M | issue = 2 }}
- {{cite journal | vauthors = Ferguson SS, Menard L, Barak LS, Koch WJ, Colapietro AM, Caron MG | year = 1995 | title = Role of phosphorylation in agonist-promoted beta 2-adrenergic receptor sequestration. Rescue of a sequestration-defective mutant receptor by beta ARK1 | journal = J. Biol. Chem. | volume = 270 | pages = 24782–9 | pmid = 7559596 | issue = 42 | doi=10.1074/jbc.270.42.24782}}
- {{cite journal | vauthors = Willets JM, Challiss RA, Nahorski SR | year = 2003 | title = Non-visual GRKs: are we seeing the whole picture? | journal = Trends Pharmacol. Sci. | volume = 24 | pages = 626–33 | pmid = 14654303 | doi = 10.1016/j.tips.2003.10.003 | issue = 12 }}
External links
- {{Commonscatinline|Beta adrenergic receptor kinase}}