The Siderophores of Pseudomonas fluorescens 18.1 and the Importance of Cyclopeptidic Substructures for the Recognition at the Cell Surface#

Silica gel column chromatography of the EtOAc extract afforded compounds 1,4,5 while the n-hexane extract provided compounds 2, 3, 6 and 7.. Compound 1 was obtained as

A ferribactin having these structural characteristics is produced by the investigated strain, but it is accompanied by derivatives where the α -amino group of Glu is partially

So far all pyoverdins with a C-terminal cyclopeptidic substructure have in common that the ε -amino group of an in-chain Lys is bound amidically to the carboxyl group of a C-

From Pseudomonas fluorescens PL7 and PL8 structurally related pyoverdins were isolated and their primary structures were elucidated by spectroscopic methods and degradation reac-

a dihydroxyquinoline chromo- phore responsible for their fluorescence, a peptide chain comprising 6 to 12 amino acids bound to its carboxyl group, and a small dicarboxylic acid (or

Pseudomonas chlororaphis, Pyoverdin, Ferribactin By a feeding experiment with a 15 N-labelled precursor it is shown that ferribactins are transformed into pyover- dins and thus

producing pyoverdins with a C-terminal cyclopeptidic substructure, the two strains can recognize to some extent structurally different pyoverdins as long as they have also a

The structure of the pyoverdin siderophore of Pseudomonas fluorescens 1.3 was elucidated by spectroscopic methods and chemical degradation.. It shows structural similarities with