The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
ACYLPEPTIDES, THE INHIBITORS OF CYCLIC ADENOSINE 3', 5'-MONOPHOSPHATE PHOSPHODIESTERASE
III. INHIBITION OF CYCLIC AMP PHOSPHODIESTERASE
KUNIAKI HOSONOHIDEO SUZUKI
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1983 Volume 36 Issue 6 Pages 679-683

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Abstract

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.

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© Japan Antibiotics Research Association
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