Lite Version|Standard version

To gain access to this content please
Log in via your home Institution.
Log in with your member or subscriber username and password.
Download

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

Page: ^ Top