
pmid: 6814825
Publisher Summary Casein kinase I and casein kinase II are unique protein kinases that have been described in a number of mammalian and avian cells; an enzyme with properties similar to those of casein kinase I has been described in yeast and plants. The casein kinases prefer acidic substrates and appear to differ from the enzyme endogenous to the mammary gland. Casein kinases I and II are multipotential in the sense that a number of endogenous substrates have been identified for them. Other multipotential protein kinases include the cAMP-dependent and cGMP-dependent protein kinases and phosphorylase kinase. No physiological regulator for casein kinase I has been identified, but the enzyme requires Mg2+ for activity and is stimulated by monovalent cations; the cation requirement is similar for casein kinase II.
2,3-Diphosphoglycerate, Chromosomal Proteins, Non-Histone, Caseins, Membrane Proteins, Diphosphoglyceric Acids, Phosphoproteins, Substrate Specificity, Phosvitin, Adenosine Triphosphate, Glycogen Synthase, Mammary Glands, Animal, Peptide Initiation Factors, Animals, Female, Amino Acid Sequence, Phosphorylation, Casein Kinases, Protein Kinase Inhibitors, Protein Kinases
2,3-Diphosphoglycerate, Chromosomal Proteins, Non-Histone, Caseins, Membrane Proteins, Diphosphoglyceric Acids, Phosphoproteins, Substrate Specificity, Phosvitin, Adenosine Triphosphate, Glycogen Synthase, Mammary Glands, Animal, Peptide Initiation Factors, Animals, Female, Amino Acid Sequence, Phosphorylation, Casein Kinases, Protein Kinase Inhibitors, Protein Kinases
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