Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. III. Inhibition of cyclic AMP phosphodiesterase.
Acylpeptides, APD-I, -II and -III, were inhibitors of cyclic adenosine 3',5'-monophosphate (cAMP) phosphodiesterase, and their inhibition types were non-competitive. The inhibitory activity of APD-II was the most potent among them. Opening of the lactone linkage reduced the inhibitory activity to about half. The activity almost disappeared when an inhibitor or a derivative with opened lactone linkage was methylated with diazomethane. The activity was, however, restored by the addition of metal ions such as Ca2+, Mn2+, Fe2+, and Co2+. This suggests that the inhibition may be caused by a chelating action of the free carboxyl groups of glutamic acid and aspartic acid in the peptide.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors*; D000469:Alkaline Phosphatase / Q000378:metabolism; D001412:Bacillus subtilis / Q000032:analysis; D002413:Cations, Divalent; D007700:Kinetics; D009842:Oligopeptides / Q000494:pharmacology*; D010208:Papaverine / Q000494:pharmacology; D012988:Soil Microbiology; D013806:Theophylline / Q000494:pharmacology
D002413:Cations, Divalent; D009842:Oligopeptides; D013806:Theophylline; D010208:Papaverine; D000469:Alkaline Phosphatase; D015105:3',5'-Cyclic-AMP Phosphodiesterases