ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases
dc.contributor.author | Olucha, José | |
dc.contributor.author | Lamb, Audrey L. | |
dc.date.accessioned | 2017-04-28T20:47:30Z | |
dc.date.available | 2017-04-28T20:47:30Z | |
dc.date.issued | 2011-12 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23861 | |
dc.description.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. | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | This article is made available under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 United States (CC BY-NC-ND 3.0 US) License. | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/us/ | en_US |
dc.subject | Ornithine | en_US |
dc.subject | Lysine | en_US |
dc.subject | Putrescine | en_US |
dc.subject | Hydroxylase | en_US |
dc.subject | Monooxygenase | en_US |
dc.subject | N-hydroxylating | en_US |
dc.subject | Flavoprotein | en_US |
dc.subject | Siderophore | en_US |
dc.subject | Hydroxamate | en_US |
dc.subject | PvdA | en_US |
dc.subject | SidA | en_US |
dc.subject | IucD | en_US |
dc.title | Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Olucha, José | |
kusw.kuauthor | Lamb, Audrey L. | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1016/j.bioorg.2011.07.006 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3188341 | en_US |
dc.rights.accessrights | openAccess |