Loading...
Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases
Olucha, José Lamb, Audrey L.
Olucha, José
Lamb, Audrey L.
Citations
Altmetric:
Abstract
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.
Description
Date
2011-12
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Collections
Research Projects
Organizational Units
Journal Issue
Keywords
Ornithine, Lysine, Putrescine, Hydroxylase, Monooxygenase, N-hydroxylating, Flavoprotein, Siderophore, Hydroxamate, PvdA, SidA, IucD
Citation
Olucha, J., & Lamb, A. L. (2011). Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases. Bioorganic Chemistry, 39(5-6), 171–177. http://doi.org/10.1016/j.bioorg.2011.07.006