Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions.
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.
Walsh
D A
DA
School of Medicine, University of California, Davis.
Glass
D B
DB
Mitchell
R D
RD
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
D011494:Protein Kinases