A cytoplasmic, cyclic nucleotide-independent casein kinase II from Saccharomyces cerevisiae.
Two molecular forms of casein kinase II (an ATP: protein phosphotransferase, EC 2.7.1.37) from yeast were isolated and characterized. The first form was composed of three polypeptide subunits with molecular weights of 41000, 37000 and 24000. The second form contained two larger polypeptides and lacked an autophosphorylatable 24 kDa subunit. The properties of both enzyme forms were found to be practically the same in respect to the substrate and phosphate donor specificities, kinetics, their sensitivity to heparin, etc. The results obtained strongly indicate that isolated yeast casein kinase II does not necessarily require the smallest subunit for the enzyme activity.
D000255:Adenosine Triphosphate / Q000378:metabolism; D047388:Casein Kinases; D003593:Cytoplasm / Q000201:enzymology; D006160:Guanosine Triphosphate / Q000378:metabolism; D046911:Macromolecular Substances; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D046911:Macromolecular Substances; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases