Abstract
The flavin-dependent N-monooxygenase SidA from Aspergillus fumigatus catalyzes the conversion of l -ornithine to N5-hydroxy- l -ornithine. This product is incorporated into hydroxamate containing siderophores, which are iron chelators required for growth during A. fumigatus infection in mammals. The activity of SidA has been shown to be required for siderophore biosynthesis. Here, we used a colorimetric product formation assay to screen a small-molecule library for the identification of potential inhibitors of SidA. Ebselen, an organoselenium compound, was identified as an inhibitor of SidA. This compound inhibited SidA with an IC50 value of 11 ± 1 μM. Ebselen derivative, ebsulfur, was also found to inhibit SidA with an IC50 value of 40 ± 13 μM. These compounds represent a new type of inhibitors of siderophore biosynthesis.
Recommended Citation
Bufkin, K. B., & Sobrado, P. (2026). Identification of Inhibitors of an N- Monooxygenase from Aspergillus Fumigatus. Biochimie, 247, pp. 145-150. Elsevier.
The definitive version is available at https://doi.org/10.1016/j.biochi.2026.06.008
Department(s)
Arts, Languages, and Philosophy
Publication Status
Full Text Access
Keywords and Phrases
Aspergillus fumigatus; Drug discovery; Flavin-dependent monooxygenases; Siderophores
International Standard Serial Number (ISSN)
6183-1638; 0300-9084
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2026 Elsevier, All rights reserved.
Publication Date
01 Aug 2026
PubMed ID
42285434
