Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis

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dc.contributor.authorBufkin, Kendraen
dc.contributor.authorSobrado, Pabloen
dc.contributor.departmentBiochemistryen
dc.contributor.departmentCenter for Drug Discoveryen
dc.date.accessioned2017-11-29T20:20:13Zen
dc.date.available2017-11-29T20:20:13Zen
dc.date.issued2017-10-01en
dc.date.updated2017-11-24T11:58:52Zen
dc.description.abstract<i>N</i>-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 <i>Amycolatopsis alba</i> growing under iron-limiting conditions. This work focuses on the expression, purification, and characterization of the NMO, abachelin monooxygenase (AMO) from <i>A. alba</i>. 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.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationBufkin, K.; Sobrado, P. Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis. Molecules 2017, 22, 1652.en
dc.identifier.doihttps://doi.org/10.3390/molecules22101652en
dc.identifier.urihttp://hdl.handle.net/10919/80565en
dc.language.isoenen
dc.publisherMDPIen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectflavinen
dc.subjectsiderophoresen
dc.subjectAmycolatopsis albaen
dc.subjectornithine hydroxylaseen
dc.titleCharacterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesisen
dc.title.serialMoleculesen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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