CATH Classification

Domain Context

CATH Clusters

Superfamily FAD/NAD(P)-binding domain
Functional Family L-ornithine N(5)-monooxygenase

Enzyme Information
L-ornithine N(5)-monooxygenase (NAD(P)H).
based on mapping to UniProt E9QYP0
L-ornithine + NAD(P)H + O(2) = N(5)-hydroxy-L-ornithine + NAD(P)(+) + H(2)O.
-!- The enzyme from the pathogenic fungus Aspergillus fumigatus catalyzes a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics. -!- Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP(+) (but not NAD(+)) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate. -!- Cf. EC

UniProtKB Entries (1)

Aspergillus fumigatus Af293
L-ornithine N(5)-monooxygenase

PDB Structure

PDB 4B67
External Links
Primary Citation
Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases.
Franceschini, S., Fedkenheuer, M., Vogelaar, N.J., Robinson, H.H., Sobrado, P., Mattevi, A.