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Beta-adrenergic-receptor kinase
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Beta-adrenergic-receptor kinase : ウィキペディア英語版
Beta-adrenergic-receptor kinase

In enzymology, a beta-adrenergic-receptor kinase () is an enzyme that catalyzes the chemical reaction:
:ATP + (receptor ) \rightleftharpoons ADP + phospho-(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:(receptor ) phosphotransferase. Other names in common use include ATP:beta-adrenergic-receptor phosphotransferase, () 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==

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抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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