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Keyword
- alkaline phosphatase1
- bacterial metabolism1
- BCCP1
- biosynthesis1
- biotin carboxyl carrier protein1
- CAA1
- casamino acid1
- EDDHA1
- ethylene diamine-N,N'-bis(2-hydroxyphenylacetic acid)1
- hrDP1
- human renal dipeptidase1
- membrane protein1
- periplasm1
- PhoA1
- Pseudomonas aeruginosa1
- Pseudomonas fluorescens1
- pyoverdine maturation1
- siderophore1
Microbiology
1 Results
- Research ArticleOpen Access
PvdM of fluorescent pseudomonads is required for the oxidation of ferribactin by PvdP in periplasmic pyoverdine maturation
Journal of Biological ChemistryVol. 298Issue 8102201Published online: June 25, 2022- Michael-Frederick Sugue
- Ali Nazmi Burdur
- Michael T. Ringel
- Gerald Dräger
- Thomas Brüser
Cited in Scopus: 0Fluorescent pseudomonads such as Pseudomonas aeruginosa or Pseudomonas fluorescens produce pyoverdine siderophores that ensure iron-supply in iron-limited environments. After its synthesis in the cytoplasm, the nonfluorescent pyoverdine precursor ferribactin is exported into the periplasm, where the enzymes PvdQ, PvdP, PvdO, PvdN, and PtaA are responsible for fluorophore maturation and tailoring steps. While the roles of all these enzymes are clear, little is known about the role of PvdM, a human renal dipeptidase–related protein that is predicted to be periplasmic and that is essential for pyoverdine biogenesis.