A flavoprotein (FAD). The enzyme is involved in biosynthesis of N5-hydroxy-L-ornithine, N5-formyl-N5-hydroxy-L-ornithine or N5-acetyl-N5-hydroxy-L-ornithine. These nonproteinogenic amino acids are building blocks of siderophores produced by some bacteria (e.g. Streptomyces coelicolor, Saccharopolyspora erythraea and Pseudomonas aeruginosa). The enzyme is specific for NADPH. cf. EC 18.104.22.168, L-ornithine N5-monooxygenase [NAD(P)H].
Ge, L. and Seah, S.Y. Heterologous expression, purification, and characterization of an l-ornithine N5-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J. Bacteriol.188 (2006) 7205–7210. [PMID: 17015659]
Meneely, K.M. and Lamb, A.L. Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism. Biochemistry46 (2007) 11930–11937. [PMID: 17900176]
Pohlmann, V. and Marahiel, M.A. δ-amino group hydroxylation of L-ornithine during coelichelin biosynthesis. Org. Biomol. Chem.6 (2008) 1843–1848. [PMID: 18452021]
Robbel, L., Helmetag, V., Knappe, T.A. and Marahiel, M.A. Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin. Biochemistry50 (2011) 6073–6080. [PMID: 21650455]