Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. III. Inhibition of cyclic AMP phosphodiesterase.
- 1 January 1983
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 36 (6), 679-683
- https://doi.org/10.7164/antibiotics.36.679
Abstract
Acylpeptides, APD-I, -II and -III [from Bacillus subtilis], were inhibitors of cAMP phosphodiesterase, and their inhibition types were non-competitive. The inhibitory activity of APD-II was the most potent. Opening of the lactone linkage reduced the inhibitory activity to about 1/2. The activity almost disappeared when an inhibitor or a derivative with opened lactone linkage was methylated with diazomethane. The activity was restored by the addition of metal ions such as Ca2+, Mn2+, Fe2+ and Co2+. The inhibition may be caused by a chelating action of the free carboxyl groups of Glutamic and Aspartic acid in the peptide.This publication has 6 references indexed in Scilit:
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