Abstract
MOST hormones and neurotransmitters are thought to stimulate the synthesis of adenosine 3′,5′-cyclic monophosphate (cyclic AMP) which in turn activates protein kinases1. On activation, the protein kinases transfer the terminal phosphate group of ATP to serine or threonine residues in enzymic or membrane proteins involved in metabolic regulation, thereby either activating or inactivating them. Only a few key proteins are phosphorylated1,2 which raises the question of the molecular basis for the recognition of a particular serine by the cyclic AMP-dependent protein kinases. Cohen et al.2 considered this problem with respect to the phosphorylation of phosphorylase kinase and glycogen synthetase and concluded that the cyclic AMP-dependent protein kinase recognises some specific three-dimensional configuration formed by a particular amino acid sequence at the site of phosphorylation. The features of this structure, however, remain to be defined. It has been shown3 that small peptides from myelin basic protein could act as substrates, thus reducing the number of parameters for consideration.
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DAILE, P., CARNEGIE, P. & YOUNG, J. Synthetic substrate for cyclic AMP-dependent protein kinase. Nature 257, 416–418 (1975). https://doi.org/10.1038/257416a0
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DOI: https://doi.org/10.1038/257416a0
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