CK2 is a serine/threonine (Ser/Thr) protein kinase that can operate as a tetrameric holoenzyme consisting of two catalytically active subunits α and/or α′ and a dimer of regulatory β-subunits or as a monomeric catalytic subunit (α or α′). Its original name “casein kinase 2,” which was derived from CK2 being identified as a kinase capable of phosphorylating casein in vitro, proved to be a misnomer since casein was found not to be a physiologic substrate of CK2.
CK2 was the first protein kinase to be identified in 1954 by Eugene Kennedy, who described the enzyme’s ability to catalyze the phosphorylation of protein substrate by ATP. CK2 possesses several distinct features that distinguish it from the majority of other kinases. It is a highly acidophilic Ser/Thr kinase that atypically phosphorylates tyrosine (Tyr) residues in addition to Ser and Thr and can also utilize GTP, besides ATP, as a phosphate donor. CK2...
KeywordsCasein Kinase Ellagic Acid Cyclic Peptide Bile Duct Cancer Selective Small Molecule Inhibitor
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