title: Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. II. Amino acid sequence and location of lactone linkage.
abstract: Bacillus subtilis C-756 produced three kinds of inhibitors of cyclic adenosine 3',5'-monophosphate (cAMP) phosphodiesterase. Each was an acylpeptide consisting of a beta-hydroxy fatty acid residue and heptapeptide. By the application of mass spectrometry, the amino acid sequence of peptide was determined to be beta-hydroxy fatty acid-Glu-Leu-Leu-Val-Asp-Leu-Leu in all three cases. Each had a lactone linkage between the carboxyl group of C-terminal leucine and the beta-hydroxyl group of the fatty acid moiety. The total structures of these inhibitors were thus established.
mesh_terms: D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors*; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000032:analysis*; D007783:Lactones / Q000032:analysis; D013058:Mass Spectrometry; D008745:Methylation; D009842:Oligopeptides / Q000302:isolation & purification* / Q000494:pharmacology; D012988:Soil Microbiology; D013329:Structure-Activity Relationship
chemical_list: D007783:Lactones; D009842:Oligopeptides; D015105:3',5'-Cyclic-AMP Phosphodiesterases