1.14.13.196: L-ornithine N5-monooxygenase [NAD(P)H]
This is an abbreviated version!
For detailed information about L-ornithine N5-monooxygenase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
abachelin monooxygenase, AfSidA, AMO, SidA, siderophore A
ECTree
1.14.13.196 L-ornithine N5-monooxygenase [NAD(P)H]Advanced search results
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results (Substrates Products
Substrates Products on EC 1.14.13.196 - L-ornithine N5-monooxygenase [NAD(P)H]
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-ornithine + NAD(P)H + H+ + O2
N5-hydroxy-L-ornithine + NAD(P)+ + H2O
Q5SE95
the enzyme catalyzes the hydroxylation of L-ornithine in ferrichrome biosynthesis
-
-
?
additional information
?
-
-
holo (FAD-bound) and apo (FAD-free) forms of the enzyme hydroxylate ornithine. No activity with L-lysine. The enzyme displays very low selectivity for the reduced nicotinamide coenzyme
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
-
-
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
first step in the biosynthesis of hydroxamate-containing siderophores, essential for virulence
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
the enzyme catalyzes the generation of N5-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
the enzyme is essential for virulence in Aspergillus fumigatus
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
accepts reducing equivalents from either NADPH or NADH and displays similar kinetic parameters when using either coenzyme
-
-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
AfSidA is highly specific for its amino acid substrate, only hydroxylating L-ornithine. An 8-fold preference in the catalytic efficiency is determined for NADPH compared to NADH
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
first step in the biosynthesis of hydroxamate-containing siderophores, essential for virulence
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
the enzyme catalyzes the generation of N5-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
the enzyme catalyzes the hydroxylation of ornithine in the biosynthesis of hydroxamate siderophores that are essential for virulence
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
the enzyme is essential for virulence in Aspergillus fumigatus
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
accepts reducing equivalents from either NADPH or NADH and displays similar kinetic parameters when using either coenzyme
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
AfSidA is highly specific for its amino acid substrate, only hydroxylating L-ornithine. An 8-fold preference in the catalytic efficiency is determined for NADPH compared to NADH
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
in the reductive half-reaction, the oxidized FAD bound to the enzyme, is reduced by NADPH. In the oxidative half-reaction, the reduced cofactor reacts with molecular oxygen to form a C4a-hydroperoxyflavin intermediate, which transfers an oxygen atom to ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
NADPH reduces the flavin, and the resulting NADP+ is the last product to be released
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-
?
