Crystallographic Studies of the Catalytic Subunit of cAMP- Dependent Protein Kinase
The cAMP-dependent protein kinase (reviewed in Beebe and Corbin, 1986) is a tetrameric enzyme, probably ubiquitous in eukaryotic cells, composed of two regulatory and two catalytic (C) subunits. Upon binding cAMP the regulatory dimer releases two monomeric C-subunits, which then use MgATP to phosphorylate serine or threonine residues found typically in the sequence Arg-Arg-X-Ser/Thr in target proteins. Protein phosphorylation is a well-known mechanism for regulating protein function (reviewed in Krebs, 1985), and a large number of proteins have been found whose activity the C-subunit regulates this way, including many from the glycolytic and gluconeogenetic pathways (Krebs, 1985).
KeywordsCatalytic Subunit Nucleotide Binding Site Dependent Protein Kinase Porcine Heart Hexagonal Form
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