Home  |  Contact

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
BRENDA1.14.13.196
EC2PDB1.14.13.196
ExplorEnz1.14.13.196
PRIAM enzyme-specific profiles1.14.13.196
KEGG Ligand Database for Enzyme Nomenclature1.14.13.196
IUBMB Enzyme Nomenclature1.14.13.196
IntEnz1.14.13.196
MEDLINEFind literature relating to 1.14.13.196
MetaCyc1.14.13.196
UniProtKB/Swiss-Prot
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;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.13.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-