[Mechanism of cAMP-dependent protein kinase activation. Covalent modification of the holoenzyme by dimethylsuberimidate].
Modification of the holoenzyme of cAMP-dependent protein kinase from porcine brain by dimethylsuberimidate was studied. It was demonstrated that a protein conjugate with a molecular mass of 180,000 Da and a stoichiometric formula of R2C2 evolves as a result of intermolecular cross-link formation in the holoenzyme molecule. The regulatory subunit partly protects the catalytic subunit from the inhibition by dimethylsuberimidate. The cross-linked holoenzyme retains the ability to be activated by cAMP. The experimental data testify to the non-identity of activation and dissociation of protein kinase.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D004120:Dimethyl Suberimidate / Q000494:pharmacology*; D004789:Enzyme Activation; D007096:Imidoesters / Q000494:pharmacology*; D066298:In Vitro Techniques; D007700:Kinetics; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine
D003432:Cross-Linking Reagents; D007096:Imidoesters; D004120:Dimethyl Suberimidate; D011494:Protein Kinases
Mekhanizm aktivatsii cAMP-zavisimoĭ proteinkinazy. Kovalentnaia modifikatsiia kholofermenta dimetilsuberimidatom.