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- W4251750237 abstract "Protein kinases catalyze the transfer of the γ-phosphate of a nucleoside triphosphate to form the phosphomonoesters of amino acid residues of a substrate polypeptide. Protein kinases are probably present in all eukaryotic cells, although most is known for the enzymes of vertebrates. In the cells of higher species, protein kinases are to be found in diverse cellular compartments. The isozymes of protein kinases can also exist and it is exemplified by the two well-characterized enzymes: cAMP-dependent protein kinase and phosphorylase kinase. Specificity for protein substrates is central to the function of protein kinases. The assessment of the selectivity of a protein kinase, however, must be made at both chemical and biological levels. Another aspect of protein kinase specificity is the phenomenon of autophosphorylation. Most protein kinases studied can catalyze the phosphorylation of one or more constituent subunits. Autophosphorylation is detected using purified enzymes at relatively high concentrations under conditions that are not physiological. In some cases, autophosphorylation can affect protein kinase activity." @default.
- W4251750237 created "2022-05-12" @default.
- W4251750237 creator A5076217348 @default.
- W4251750237 date "1984-01-01" @default.
- W4251750237 modified "2023-09-25" @default.
- W4251750237 title "Protein kinases" @default.
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- W4251750237 doi "https://doi.org/10.1016/0076-6879(84)07006-3" @default.
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- W4251750237 hasPublicationYear "1984" @default.
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