title: An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase.
abstract: Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.
mesh_terms: D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D000242:Cyclic AMP / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000302:isolation & purification; D010446:Peptide Fragments / Q000302:isolation & purification* / Q000494:pharmacology; D047428:Protein Kinase Inhibitors; D012697:Serine Endopeptidases; D013211:Staphylococcus aureus / Q000201:enzymology
chemical_list: D004791:Enzyme Inhibitors; D010446:Peptide Fragments; D047428:Protein Kinase Inhibitors; D000242:Cyclic AMP; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase