[Cyclic AMP-dependent pig brain protein kinase: subunit structure, mechanism of autophosphorylation and holoenzyme dissociation under cyclic AMP action].
Some properties of cyclic AMP-dependent pig brain protein kinase were studied. The holoenzyme was shown to exist in solution in the form of a tetramer complex R2C2 with mol. weight of 180 000. The limited proteolysis of the regulatory subunit caused the formation of a fragment with mol. weight of 35 000, capable of independent binding of 3H-cyclic AMP and containing a site, which can be phosphorylated in the autophosphorylation reaction. Autophosphorylation of the holoenzyme led to an increase in the degree of dissociation of the former into individual subunits under the effect of cyclic AMP. The ability of the phosphoform of the catalytic subunit was demonstrated. The autophosphorylation process and the phosphotransferase reaction involve the same active site of the catalytic subunit.
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology*; D000242:Cyclic AMP / Q000494:pharmacology*; D004789:Enzyme Activation; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine
D046911:Macromolecular Substances; D000242:Cyclic AMP; D011494:Protein Kinases
cAMP-zavisimaia proteinkinaza iz mozga svin'i: subdedinichnaia struktura, mekhanizm avtofosforilirovaniia i dissotsiatsiia na subdedinitsy pod deĭstviem cAMP.