Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSA

The ornithine hydroxylase from Pseudomonas aeruginosa (PvdA) catalyzes the FAD-dependent hydroxylation of the side chain amine of ornithine, which is subsequently formylated to generate the iron-chelating hydroxamates of the siderophore pyoverdin. PvdA belongs to the class B flavoprotein monooxygena...

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Hlavní autoři: Olucha, Jose, Meneely, Kathleen M., Chilton, Annemarie S., Lamb, Audrey L.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2011
Témata:
Enzymology
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3173084/
https://ncbi.nlm.nih.gov/pubmed/21757711
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.265876
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