title: Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions.
abstract: The proposition is forwarded that the cAMP-dependent protein kinase is one of quite a small class of enzymes wherein differential modes of binding of its multiple substrates make an important contribution to the end physiological response. It is postulated that a variety of different substrate affinities may have evolved in order to regulate the order of substrate phosphorylation. The recent elucidation of the protein's three-dimensional structure provides the opening to test this as a new concept of cellular regulation.
authors.affiliation: School of Medicine, University of California, Davis.
authors.forename: D A
authors.initials: DA
authors.lastname: Walsh
authors.forename: D B
authors.initials: DB
authors.lastname: Glass
authors.forename: R D
authors.initials: RD
authors.lastname: Mitchell
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011494:Protein Kinases