Abstract
Protein phosphorylation is a common posttranslational modification associated with regulatory processes in eukaryotic cells. Protein kinases represent a large and diverse family of enzymes that catalyze the transfer from the γ-phosphate of ATP to a target protein or peptide. These enzymes regulate most known metabolic pathways by phosphorylating either a serine, threonine or tyrosine residue (Krebs & Beavo, 1979). The first protein kinase to be discovered was phosphorylase kinase (Krebs et al., 1959), but the best understood biochemically is the second to be described, cAMP-dependent protein kinase (cAPK) (Walsh et al., 1968). cAPK is one of the simplest and smallest in the large family of protein kinases, which overall show tremendous diversity in terms of size, subunit structure, subcellular localization, and activation mechanism. Despite these differences, however, all eukaryotic protein kinases, including the catalytic subunit of the cAPK, share a conserved catalytic core (Hanks et al., 1988). For this reason, the C-subunit can serve as a framework for the entire protein kinase family (Taylor et al., 1992).
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© 1993 Springer-Verlag Berlin Heidelberg
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Herberg, F.W., Yonemoto, W., Taylor, S.S. (1993). The Catalytic Subunit of cAMP-Dependent Protein Kinase. In: Heilmeyer, L.M.G. (eds) Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling. NATO ASI Series, vol 76. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78247-3_25
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DOI: https://doi.org/10.1007/978-3-642-78247-3_25
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