Journal
BIOORGANIC CHEMISTRY
Volume 39, Issue 4-6, Pages 171-177Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2011.07.006
Keywords
Ornithine; Lysine; Putrescine; Hydroxylase; Monooxygenase; N-hydroxylating; Flavoprotein; Siderophore; Hydroxamate; PvdA; SidA; IucD
Funding
- National Institute of General Medical Sciences [T32 GM08545]
- NIH from National Institute for Allergy and Infectious Disease [K02 A1093675]
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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. (C) 2011 Elsevier Inc. All rights reserved.
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