ENZYME entry: EC 1.14.13.196
Accepted Name |
L-ornithine N(5)-monooxygenase (NAD(P)H).
|
Reaction catalysed |
L-ornithine + NAD(P)H + O(2) <=> N(5)-hydroxy-L-ornithine + NAD(P)(+) + H(2)O |
Cofactor(s) |
FAD.
|
Comment(s) |
- 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.
|
Cross-references |
BRENDA | 1.14.13.196 |
EC2PDB | 1.14.13.196 |
ExplorEnz | 1.14.13.196 |
PRIAM enzyme-specific profiles | 1.14.13.196 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.13.196 |
IUBMB Enzyme Nomenclature | 1.14.13.196 |
IntEnz | 1.14.13.196 |
MEDLINE | Find literature relating to 1.14.13.196 |
MetaCyc | 1.14.13.196 |
Rhea expert-curated reactions | 1.14.13.196 |
UniProtKB/Swiss-Prot |
A8NF99, CPF2_COPC7; | N4WYI1, SIDA2_COCH4; | B2KWI1, SIDA_AJECA; |
D4AU57, SIDA_ARTBC; | E9QYP0, SIDA_ASPFU; | Q2TZB2, SIDA_ASPOR; |
M2PP75, SIDA_CERS8; | G5EB76, SIDA_EMENI; | I1RN13, SIDA_GIBZE; |
Q52UT0, SIDA_OMPOL; | Q9P7T0, SIDA_SCHPO; | P56584, SIDA_USTMA; |
|
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