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ENZYME

ENZYME entry: EC 1.14.13.196

Accepted Name
L-ornithine N(5)-monooxygenase [NAD(P)H]
Reaction catalysed
  • L-ornithine + NADPH + O2 <=> H2O + N(5)-hydroxy-L-ornithine + NADP(+)
  • L-ornithine + NADH + O2 <=> H2O + N(5)-hydroxy-L-ornithine + NAD(+)
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
Rhea expert-curated reactions1.14.13.196
UniProtKB/Swiss-Prot
A8NF99, CPF2_COPC7N4WYI1, SIDA2_COCH4B2KWI1, SIDA_AJECA
D4AU57, SIDA_ARTBCE9QYP0, SIDA_ASPFUQ2TZB2, SIDA_ASPOR
M2PP75, SIDA_CERS8G5EB76, SIDA_EMENII1RN13, SIDA_GIBZE
Q52UT0, SIDA_OMPOLQ9P7T0, SIDA_SCHPOP56584, SIDA_USTMA

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