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Molecules 2017, 22(10), 1652; doi:10.3390/molecules22101652

Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis

1
Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA
2
Center for Drug Discovery, Virginia Tech, Blacksburg, VA 24061, USA
*
Author to whom correspondence should be addressed.
Received: 7 September 2017 / Revised: 27 September 2017 / Accepted: 28 September 2017 / Published: 1 October 2017
(This article belongs to the Special Issue Flavoenzymes)
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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. View Full-Text
Keywords: flavin; siderophores; Amycolatopsis alba; ornithine hydroxylase flavin; siderophores; Amycolatopsis alba; ornithine hydroxylase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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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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