L-ornithine N5 monooxygenase
| L-ornithine N5 monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Ornithine monooxygenase tetramer, Aspergillus fumigatus | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.13.196 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an ornithine monooxygenase (EC 1.14.13.196) is an enzyme that catalyzes the chemical reaction
- L-ornithine + NAD(P)H + O2 N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O
Thus, the three substrates of this enzyme are L-ornithine, NAD(P)H and O2, whereas its three products are N(5)-hydroxy-L-ornithine, NAD(P)+ and H2O. The coenzyme is FAD.
This enzyme belongs to the family of oxidoreductases, specifically the monooxygenases. The systematic name of this enzyme class is L-ornithine N5 monooxygenase (flavin-dependent). 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 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics.
Structural studies
As of late 2013, 8 structures have been solved for this class of enzymes, with PDB accession codes 4NZH, 4B63, 4B64, 4B65, 4B66, 4B67, 4B68 and 4B69.
References
- Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A (2012). "Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases". Biochemistry. 51: 7043–5. doi:10.1021/bi301072w. PMID 22928747.
- http://www.jbc.org/content/early/2013/09/26/jbc.M113.487181.full.pdf
