Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. II. Amino acid sequence and location of lactone linkage.
- 1 January 1983
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 36 (6), 674-678
- https://doi.org/10.7164/antibiotics.36.674
Abstract
Bacillus subtilis C-756 produced 3 kinds of inhibitors of 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 3 cases. Each had a lactone linkage between the carboxyl group of C-terminal Leu and the .beta.-hydroxl group of the fatty acid moiety. The total structures of these inhibitors were established.This publication has 4 references indexed in Scilit:
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