Amino Acid Sequence; Amino Acids/analysis; Biotransformation; Isoelectric Focusing; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Oligopeptides/chemistry/isolation & purification/metabolism; Pigments, Biological/biosynthesis; Pseudomonas putida/growth & development/metabolism; Siderophores; Spectrometry, Mass, Fast Atom Bombardment
Abstract :
[en] Pyoverdin type siderophores produced by six fluorescent Pseudomonas strains isolated from different rhizospheres were purified and characterized. The purified ferri-pyoverdins were tested for their ability to promote the growth of other strains grown under iron deficiency conditions. Only the one obtained from Pseudomonas putida BTP1 did not act as a growth promoter. The structure of the BTP1 siderophore was elucidated by spectroscopic methods and degradation studies. It turned out that it contains a chromophore which differs from the one typical for pyoverdins insofar as it carries the carboxyl group in 3- rather than in 1-position ((3S)-5-amino-1,2-dihydro-8,9-dihydroxy-3H-pyrimido[1,2a]quinoline-3- carboxylic acid). The amino group of the chromophore is substituted with the 5-carboxyl group of L-glutamic acid and its carboxyl group with the N-terminus of the peptide L-Asp-L-Ala-L-Asp-D-N5-Ac-N5-OH-Orn-L-Ser-L-c-N5-OH-Orn. This isopyoverdin fits into the biogenetic scheme which postulates ferribactins as the precursors of pyoverdins.
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