Expression of L-ornithine N δ -oxygenase (PvdA) in fluorescent Pseudomonas species: An immunochemical and in silico study

Lorenza Putignani, Cecilia Ambrosi, Paolo Ascenzi, Paolo Visca

Research output: Contribution to journalArticlepeer-review


ω-Amino acid monooxygenases (EC 1.14.13.-), catalysing the formation of hydroxamate precursors of microbial siderophores (e.g., pyoverdine), have so far eluded structural and biochemical characterisation. Here, the expression of recombinant L-ornithine-Nδ-oxygenase (PvdA) from Pseudomonas aeruginosa PAO1 is reported. A library of eight monoclonal antibodies (MAbs) directed against PvdA has been generated. Two MAb families recognising the N- and C-terminal regions of PvdA were identified. The MAbs made it possible to demonstrate that 45-48kDa PvdA homologues are expressed in response to iron limitation by different species and strains of fluorescent pseudomonads. Despite the different degrees in sequence similarity between P. aeruginosa PvdA and putative homologues from Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas syringae, Burkholderia cepacia, and Ralstonia solanacearum, in silico domain scanning predicts an impressive conservation of putative cofactor and substrate binding domains. The MAb library was also used to monitor PvdA expression during the transition of P. aeruginosa from iron-sufficient to iron-deficient growth.

Original languageEnglish
Pages (from-to)245-257
Number of pages13
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Jan 9 2004


  • ω-Amino acid monooxygenases
  • Iron regulation
  • Monoclonal antibodies
  • Pseudomonas
  • PvdA
  • Pyoverdine

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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