Conformational and Shape Changes Associated with cAMP- Dependent Protein Kinase
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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).
KeywordsCatalytic Subunit Protein Kinase Inhibitor Dependent Protein Kinase Mammalian Enzyme cAMP Binding
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