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Issue 10, 2008

δ-Amino group hydroxylation of l-ornithine during coelichelin biosynthesis

Author affiliations

Abstract

The nonribosomally produced hydroxamate siderophore coelichelin from Streptomyces coelicolor contains the nonproteinogenic amino acidsN5-hydroxyornithine and N5-hydroxyformylornithine that are important for iron assembly. The hydroxylation of the δ-amino group of L-ornithine is catalyzed by the flavin-dependent monooxygenase CchB. During the redox reaction nicotinamide adenine dinucleotide phosphate (NADPH) and molecular oxygen are consumed and flavin adenine dinucleotide (FAD) is needed as a cofactor. During this work the monooxygenase was biochemically characterized and it could be shown that the hydroxylation of L-ornithine is most likely the first step in the biosynthesis of the siderophore coelichelin.

Graphical abstract: δ-Amino group hydroxylation of l-ornithine during coelichelin biosynthesis

Article information


Submitted
18 Jan 2008
Accepted
29 Feb 2008
First published
04 Apr 2008

Org. Biomol. Chem., 2008,6, 1843-1848
Article type
Paper

δ-Amino group hydroxylation of L-ornithine during coelichelin biosynthesis

V. Pohlmann and M. A. Marahiel, Org. Biomol. Chem., 2008, 6, 1843 DOI: 10.1039/B801016A

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