Abstract
The structure of the corpeptins, bioactive lipodepsipeptides produced in culture by Pseudomonas corrugata, the causal agent of tomato pith necrosis, has been determined. The combined use of FAB-mass spectrometry, NMR spectroscopy and chemical procedures has allowed us to assign the following primary structyre to the peptide moiety: Dhb-Pro-Ala-Ala-AlaVal-Val-Dhb-Hse-Val- aIle-Dhp-Ala-Ala-Ala-Val-Dhb- aThr-Ala-Dab-Ser-Ile with the terminal carboxy group closing a macrocyclic ring on the hydroxy group of the allo-threonine residue. The N-terminus is in turn acylated by 3-hydroxydecanoate in corpeptin A and by cis-3-hydroxy-5-dodecenoate in corpeptin B. Some preliminary data on the biological activity of corpeptins are included. © 1998 Federation of European Biochemical Societies.
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