Abstract
SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N5-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP+, and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes. © 2012 American Chemical Society.
Recommended Citation
S. Franceschini et al., "Structural Insight into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-dependent N-hydroxylating Monooxygenases," Biochemistry, vol. 51, no. 36, pp. 7043 - 7045, American Chemical Society, Sep 2012.
The definitive version is available at https://doi.org/10.1021/bi301072w
Department(s)
Chemistry
International Standard Serial Number (ISSN)
1520-4995; 0006-2960
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 American Chemical Society, All rights reserved.
Publication Date
11 Sep 2012
PubMed ID
22928747
