CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family | L-ornithine N(5)-monooxygenase |
Enzyme Information
| 1.14.13.196 |
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 1.14.13.195.
|
UniProtKB Entries (1)
| E9QYP0 |
SIDA_ASPFU
Aspergillus fumigatus Af293
L-ornithine N(5)-monooxygenase
|
PDB Structure
| PDB | 4B67 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases.
Biochemistry
|
