| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1355727 | Bioorganic Chemistry | 2011 | 7 Pages |
The N-hydroxylating flavoprotein monooxygenases are siderophore biosynthetic enzymes that catalyze the hydroxylation of the sidechain amino-group of ornithine or lysine or the primary amino-group of putrescine. This hydroxylated product is subsequently formylated or acylated and incorporated into the siderophore. Importantly, the modified amino-group is a hydroxamate and serves as an iron chelating moiety in the siderophore. This review describes recent work to characterize the ornithine hydroxylases from Pseudomonas aeruginosa (PvdA) and Aspergillus fumigatus (SidA) and the lysine hydroxylase from Escherichia coli (IucD). This includes summaries of steady and transient state kinetic data for all three enzymes and the X-ray crystallographic structure of PvdA.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► N-hydroxylating flavoprotein monooxygenases in hydroxamate siderophore biosynthesis. ► Review of kinetic studies revealing mechanism. ► Review of structural studies revealing FAD, NADPH and substrate binding/specificity.
