PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.

@article{Kenji2019PvdFOP,
  title={PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.},
  author={Nikola Kenji{\'c} and Matthew Robert Hoag and Garrett C. Moraski and Carol A. Caperelli and Graham R. Moran and Audrey L. Lamb},
  journal={Archives of biochemistry and biophysics},
  year={2019},
  volume={664},
  pages={
          40-50
        }
}
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Identification of Active Site Residues of the Siderophore Synthesis Enzyme PvdF and Evidence for Interaction of PvdF with a Substrate-Providing Enzyme
TLDR
A co-purification assay showed that PvdF binds to an enzyme PvdA that catalyses synthesis of hydroxyornithine, with this interaction likely to increase the efficiency of fOHOrn synthesis, advance understanding of how P. aeruginosa synthesises pyoverdine, a key factor in host–pathogen interactions.
Nonribosomal Peptide Synthesis Definitely Working Out of the Rules
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A constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribsomal peptides.
Biosynthetic Pathways to Nonproteinogenic α-Amino Acids.
TLDR
Recently discovered biosynthetic routes to freestanding nonproteinogenic α-amino acids are reviewed, with an emphasis on work reported between 2013 and mid-2019.

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