EC |
1.14.13.195 |
Accepted name: |
L-ornithine N5-monooxygenase (NADPH) |
Reaction: |
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O |
Other name(s): |
CchB; ornithine hydroxylase; EtcB; PvdA; Af-OMO; dffA (gene name) |
Systematic name: |
L-ornithine,NADPH:oxygen oxidoreductase (N5-hydroxylating) |
Comments: |
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 1.14.13.196, L-ornithine N5-monooxygenase [NAD(P)H]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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. [DOI] [PMID: 17015659] |
2. |
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. Biochemistry 46 (2007) 11930–11937. [DOI] [PMID: 17900176] |
3. |
Pohlmann, V. and Marahiel, M.A. δ-amino group hydroxylation of L-ornithine during coelichelin biosynthesis. Org. Biomol. Chem. 6 (2008) 1843–1848. [DOI] [PMID: 18452021] |
4. |
Robbel, L., Helmetag, V., Knappe, T.A. and Marahiel, M.A. Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin. Biochemistry 50 (2011) 6073–6080. [DOI] [PMID: 21650455] |
|
[EC 1.14.13.195 created 2014] |
|
|
|
|