Abstract
Cyclic-AMP dependent protein kinase (cAPK) was one the first discovered protein kinases (Walsh et al., 1968) and is one of the best understood biochemically of the protein kinases (Taylor et al., 1990). cAPK is composed of both regulatory (R) and catalytic (C) subunits. In the absence of cAMP the subunits associate with a high affinity to form an inactive tetrameric (R2C2) holoenzyme. cAMP binds to the R-subunit promoting the dissociation of the complex into a dimeric R-subunit and two monomeric active C-subunits which transfer the γ-phosphate of ATP to a serine or threonine of a peptide or protein substrate (Beebe and Corbin, 1986).
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© 1991 Springer-Verlag Berlin Heidelberg
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Herberg, F.W., Taylor, S.S. (1991). Conformational and Shape Changes Associated with cAMP- Dependent Protein Kinase. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_14
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DOI: https://doi.org/10.1007/978-3-642-75142-4_14
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