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- W2757150947 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." @default.
- W2757150947 created "2017-10-06" @default.
- W2757150947 creator A5090367829 @default.
- W2757150947 date "2017-10-01" @default.
- W2757150947 modified "2023-10-01" @default.
- W2757150947 title "Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis" @default.
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- W2757150947 doi "https://doi.org/10.3390/molecules22101652" @default.
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