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  • Title: Specificity determinants of maize casein kinase-IIB are related to but distinct from those of rat liver casein kinase-2.
    Author: Dobrowolska G, Meggio F, Marchiori F, Pinna LA.
    Journal: Biochim Biophys Acta; 1989 Feb 09; 1010(2):274-7. PubMed ID: 2912506.
    Abstract:
    The site specificity of maize seedling casein kinase-IIB, a type-2 casein kinase exhibiting an unusually low Mr, has been studied with the aid of model acidic peptide substrates for rat liver casein kinase-2. Like the animal enzyme, casein kinase-IIB also readily phosphorylates peptides SEEEEE, SEAEEE and SEEEAE, but not SEEAEE. Maize seedling casein kinase-IIB, however, is almost inactive toward peptides SAEEEE, SAEEEEE and SAAEEEEE which are good substrates for liver casein kinase-2. This indicates that casein kinase-IIB requires acidic residues not only at position +3, similar to rat liver casein kinase-2, but also at position +1, where the animal enzyme tolerates a neutral residue. This and other differences outlined in this report support the view that protein kinases of the same type from different sources may have significant differences in their substrate specificity.
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