Abstract
N-Hydroxylating monooxygenases (NMOs) are involved in siderophore biosynthesis. Siderophores are high affinity iron chelators composed of catechol and hydroxamate functional groups that are synthesized and secreted by microorganisms and plants. Recently, a new siderophore named albachelin was isolated from a culture of Amycolatopsis alba growing under iron-limiting conditions. This work focuses on the expression, purification, and characterization of the NMO, abachelin monooxygenase (AMO) from A. alba. This enzyme was purified and characterized in its holo (FAD-bound) and apo (FAD-free) forms. The apo-AMO could be reconstituted by addition of free FAD. The two forms of AMO hydroxylate ornithine, while lysine increases oxidase activity but is not hydroxylated and display low affinity for NADPH.
Recommended Citation
K. Bufkin and P. Sobrado, "Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis," Molecules, vol. 22, no. 10, article no. 22101652, MDPI, Oct 2017.
The definitive version is available at https://doi.org/10.3390/molecules22101652
Department(s)
Chemistry
Publication Status
Open Access
Keywords and Phrases
Amycolatopsis alba; Flavin; Ornithine hydroxylase; Siderophores
International Standard Serial Number (ISSN)
1420-3049
Document Type
Article - Journal
Document Version
Final Version
File Type
text
Language(s)
English
Rights
© 2024 The Authors, All rights reserved.
Creative Commons Licensing
This work is licensed under a Creative Commons Attribution 4.0 License.
Publication Date
01 Oct 2017
PubMed ID
28974024
Comments
National Science Foundation, Grant MCB-1021384