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• W2008678908 abstract "The nonribosomally produced hydroxamate siderophore coelichelin from Streptomyces coelicolor contains the nonproteinogenic amino acids N(5)-hydroxyornithine and N(5)-hydroxyformylornithine that are important for iron assembly. The hydroxylation of the delta-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." @default.
• W2008678908 created "2016-06-24" @default.
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• W2008678908 date "2008-01-01" @default.
• W2008678908 modified "2023-10-06" @default.
• W2008678908 title "δ-Amino group hydroxylation of l-ornithine during coelichelin biosynthesis" @default.
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• W2008678908 doi "https://doi.org/10.1039/b801016a" @default.
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