Pyoverdine biosynthesis and secretion in Pseudomonas aeruginosa: implications for metal homeostasis.

@article{Schalk2013PyoverdineBA,
  title={Pyoverdine biosynthesis and secretion in Pseudomonas aeruginosa: implications for metal homeostasis.},
  author={Isabelle J. Schalk and Laurent Guillon},
  journal={Environmental microbiology},
  year={2013},
  volume={15 6},
  pages={
          1661-73
        }
}
Pyoverdines are siderophores produced by fluorescent Pseudomonads to acquire iron. At least 60 different pyoverdines produced by diverse strains have been chemically characterized. They all consist of a dihydroquinoline-type chromophore linked to a peptide. These peptides are of various lengths and the sequences are strain specific. Pyoverdine biosynthesis in Pseudomonas aeruginosa and fluorescent Pseudomonads is a complex process involving at least 12 different proteins, starting in the… 
Deciphering Protein Dynamics of the Siderophore Pyoverdine Pathway in Pseudomonas aeruginosa
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It is shown that most of the proteins involved in the PVD pathway are homogeneously distributed throughout the bacterial cell, and the first diffusion coefficients ever determined in P. aeruginosa are determined.
The biosynthesis of pyoverdines
TLDR
The current knowledge of pyoverdine biosynthesis is reviewed with a focus on the recent advancements regarding the periplasmic maturation and tailoring reactions.
Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases
TLDR
The structural basis of PvdP's activity in PVD biosynthesis is unraveled, observations that may inform structure-guided development of PvDP-specific inhibitors to manage P. aeruginosa infections.
PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa
TLDR
P, a periplasmic enzyme of previously unknown function, is a tyrosinase required for the maturation of the pyoverdine chromophore in Pseudomonas aeruginosa and represents the first characterized member of a small family of tyros inases present in fluorescent pseudomonads that are required for siderophore maturation and are capable of acting on large peptidic substrates.
The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to α-ketoglutaric acid
TLDR
The identification and characterization of a periplasmic transaminase in fluorescent pseudomonads and other proteobacteria that is not restricted to pyoverdine-producing bacteria is reported, suggesting it is a general tool for specific biosynthetic pathways.
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TLDR
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Pyoverdines Are Essential for the Antibacterial Activity of Pseudomonas chlororaphis YL-1 under Low-Iron Conditions
TLDR
The results demonstrated that PVDs are essential for the broad-spectrum antibacterial activities of strain YL-1 against both Gram-positive and Gram-negative bacteria under low-iron conditions and that with the increase of iron, its PVD production and antibacterial activity were reduced.
Selectivity of pyoverdine recognition by the FpvA receptor of Pseudomonas aeruginosa from molecular dynamics simulations.
TLDR
Molecular dynamics and free energy calculations are used to characterize the mechanisms and thermodynamics of the recognition of the native pyoverdines of P. aeruginosa and P. fluorescens by FpvA and delineate the features that py overdines with high affinity for FpVA should possess.
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TLDR
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TLDR
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TLDR
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