Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis.
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.
Pohlmann
Verena
V
Chemistry/Biochemistry Department, Philipps-University Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
Marahiel
Mohamed A
MA
D000586:Amination; D002851:Chromatography, High Pressure Liquid; D006861:Hydrogen Peroxide / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006900:Hydroxylation; D007700:Kinetics; D013058:Mass Spectrometry; D015394:Molecular Structure; D009842:Oligopeptides / Q000096:biosynthesis* / Q000737:chemistry*; D009952:Ornithine / Q000737:chemistry*; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
D009842:Oligopeptides; C412862:coelichelin; D006861:Hydrogen Peroxide; D009952:Ornithine; D010105:Oxygenases; C020066:dimethylaniline monooxygenase (N-oxide forming)