Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis |
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Authors: | Pohlmann Verena Marahiel Mohamed A |
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Institution: | Chemistry/Biochemistry Department, Philipps-University Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. |
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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. |
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