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Microbiology
3 Results
- EnzymologyOpen Access
PvdO is required for the oxidation of dihydropyoverdine as the last step of fluorophore formation in Pseudomonas fluorescens
Journal of Biological ChemistryVol. 293Issue 7p2330–2341Published online: December 5, 2017- Michael T. Ringel
- Gerald Dräger
- Thomas Brüser
Cited in Scopus: 14Pyoverdines are important siderophores that guarantee iron supply to important pathogenic and non-pathogenic pseudomonads in host habitats. A key characteristic of all pyoverdines is the fluorescent dihydroxyquinoline group that contributes two ligands to the iron complexes. Pyoverdines are derived from the non-ribosomally synthesized peptide ferribactin, and their fluorophore is generated by periplasmic oxidation and cyclization reactions of d-tyrosine and l-diaminobutyric acid. The formation of the fluorophore is known to be driven by the periplasmic tyrosinase PvdP. - EnzymologyOpen Access
The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to α-ketoglutaric acid
Journal of Biological ChemistryVol. 292Issue 45p18660–18671Published online: September 14, 2017- Michael T. Ringel
- Gerald Dräger
- Thomas Brüser
Cited in Scopus: 8The periplasmic conversion of ferribactin to pyoverdine is essential for siderophore biogenesis in fluorescent pseudomonads, such as pathogenic Pseudomonas aeruginosa or plant growth-promoting Pseudomonas fluorescens. The non-ribosomal peptide ferribactin undergoes cyclizations and oxidations that result in the fluorophore, and a strictly conserved fluorophore-bound glutamic acid residue is converted to a range of variants, including succinamide, succinic acid, and α-ketoglutaric acid residues. We recently discovered that the pyridoxal phosphate-containing enzyme PvdN is responsible for the generation of the succinamide, which can be hydrolyzed to succinic acid. - EnzymologyOpen Access
PvdN Enzyme Catalyzes a Periplasmic Pyoverdine Modification
Journal of Biological ChemistryVol. 291Issue 46p23929–23938Published online: October 4, 2016- Michael T. Ringel
- Gerald Dräger
- Thomas Brüser
Cited in Scopus: 19Pyoverdines are high affinity siderophores produced by a broad range of pseudomonads to enhance growth under iron deficiency. They are especially relevant for pathogenic and mutualistic strains that inhabit iron-limited environments. Pyoverdines are generated from non-ribosomally synthesized highly modified peptides. They all contain an aromatic chromophore that is formed in the periplasm by intramolecular cyclization steps. Although the cytoplasmic peptide synthesis and side-chain modifications are well characterized, the periplasmic maturation steps are far from understood.