Physico-chemical principles of cAMP-dependent protein phosphorylation. Catalysis of phosphoryl group transfer to nucleophilic agents.
The specificity of pig brain protein kinase towards high- and low-Mr 'analogs' of protein substrate was studied. Solvolysis of the phosphoenzyme intermediate by various nucleophilic agents is shown. The transition state structure of the phosphoryl transfer reaction is discussed.
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology; D002625:Chemistry, Organic; D000242:Cyclic AMP / Q000378:metabolism; D007700:Kinetics; D055601:Organic Chemistry Phenomena; D010750:Phosphoproteins / Q000096:biosynthesis; D010766:Phosphorylation; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013552:Swine
D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase