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 structure to the peptide moiety: Dhb-Pro-Ala-Ala-Ala-Val-V al-Dhb-Hse-Val-alle-Dhp-Ala-Ala-Ala-Val-Dhb-aThr-Al-a-Dab-Ser-lle 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. (C) 1998 Federation of European Biochemical Societies.
Emanuele, M., Scaloni, A., Lavermicocca, P., Jacobellis, N., Camoni, L., Di Giorgio, D., et al. (1998). Corpeptins, new bioactive lipodepsipeptides from cultures of Pseudomonas corrugata. FEBS LETTERS, 433(3), 317-320.
Corpeptins, new bioactive lipodepsipeptides from cultures of Pseudomonas corrugata
CAMONI, LORENZO;PACI, MAURIZIO;
1998-01-01
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 structure to the peptide moiety: Dhb-Pro-Ala-Ala-Ala-Val-V al-Dhb-Hse-Val-alle-Dhp-Ala-Ala-Ala-Val-Dhb-aThr-Al-a-Dab-Ser-lle 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. (C) 1998 Federation of European Biochemical Societies.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
