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Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis

Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA
Center for Drug Discovery, Virginia Tech, Blacksburg, VA 24061, USA
Author to whom correspondence should be addressed.
Molecules 2017, 22(10), 1652;
Received: 7 September 2017 / Revised: 27 September 2017 / Accepted: 28 September 2017 / Published: 1 October 2017
(This article belongs to the Special Issue Flavoenzymes)
PDF [1739 KB, uploaded 18 October 2017]


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. View Full-Text
Keywords: flavin; siderophores; Amycolatopsis alba; ornithine hydroxylase flavin; siderophores; Amycolatopsis alba; ornithine hydroxylase

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Bufkin, K.; Sobrado, P. Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis. Molecules 2017, 22, 1652.

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