EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH)

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IntEnz Enzyme Nomenclature
EC 1.14.13.195

Names

Accepted name:
L-ornithine N5-monooxygenase (NADPH)
Other names:
CchB
ornithine hydroxylase
EtcB
PvdA
Af-OMO
dffA (gene name)
Systematic name:
L-ornithine,NADPH:oxygen oxidoreductase (N5-hydroxylating)

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Ge, L., Seah, S. Y.
    Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa.
    J. Bacteriol. 188: 7205-7210 (2006). [PMID: 17015659]
  2. Meneely, K. M., Lamb, A. L.
    Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.
    Biochemistry 46: 11930-11937 (2007). [PMID: 17900176]
  3. Pohlmann, V., Marahiel, M. A.
    Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis.
    Org. Biomol. Chem. 6: 1843-1848 (2008). [PMID: 18452021]
  4. Robbel, L., Helmetag, V., Knappe, T. A., Marahiel, M. A.
    Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin.
    Biochemistry 50: 6073-6080 (2011). [PMID: 21650455]

[EC 1.14.13.195 created 2014]