Information on EC 1.14.13.196 - L-ornithine N5-monooxygenase [NAD(P)H]

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The expected taxonomic range for this enzyme is: Aspergillus fumigatus

EC NUMBER
COMMENTARY hide
1.14.13.196
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RECOMMENDED NAME
GeneOntology No.
L-ornithine N5-monooxygenase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-ornithine + NAD(P)H + H+ + O2 = N5-hydroxy-L-ornithine + NAD(P)+ + H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
L-ornithine,NAD(P)H:oxygen oxidoreductase (N5-hydroxylating)
A flavoprotein (FAD). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyses 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 [3]. cf. EC 1.14.13.195, L-ornithine N5-monooxygenase (NADPH).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-ornithine + NAD(P)H + H+ + O2
N5-hydroxy-L-ornithine + NAD(P)+ + H2O
show the reaction diagram
Q5SE95
the enzyme catalyzes the hydroxylation of L-ornithine in ferrichrome biosynthesis
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-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
show the reaction diagram
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-ornithine + NAD(P)H + H+ + O2
N5-hydroxy-L-ornithine + NAD(P)+ + H2O
show the reaction diagram
Q5SE95
the enzyme catalyzes the hydroxylation of L-ornithine in ferrichrome biosynthesis
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-
?
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
show the reaction diagram
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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substrate inhibition
NADP+
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competitive inhibitor with respect to NADPH
NADPH
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substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 2
L-ornithine
0.1 - 0.94
NADH
0.012 - 0.9
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.87
L-ornithine
0.73 - 1.36
NADH
0.6 - 1.25
NADPH
additional information
additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 1.33
L-ornithine
192
1.3 - 7.3
NADH
8
14 - 50
NADPH
5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9
NADH
-
pH 7.5, 25C
2.8
NADPH
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pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
228000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 55000, SDS-PAGE; 4 * 57210, MALDI-TOF MS
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme bound to NADP+ and L-ornithine (1.9 A resolution), crystal structure of the enzyme bound to NADP+ and L-lysine (2.28 A resolution), crystal structure of the enzyme (reduced state) bound to NADPH (2.32 A resolution), crystal structure of the enzyme (reduced state) bound to NADP+ and L-arginine (2.9 A resolution), crystal structure of the enzyme (re-oxidized state) bound to NADP+ and L-ornithine (2.75 A resolution), crystal structure of the enzyme (re-oxidized state) bound to NADP+ and L-arginine (2.29 A resolution), crystal structure of the enzyme bound to L-ornithine (2.3 A resolution)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADP+, and not NAD+, protects the enzyme from proteolysis
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the presence of NADP+ is essential for activity, as it is required for stabilization of the C4a-hydroperoxyflavin, which is the hydroxylating species
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion to MBP containing an 8His tag at the N-terminus in Escherichia coli BL21T1R cells
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expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S257A
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following oxygen consumption, the Km value of the S257A enzyme for NADPH was not significantly changed, whereas the kcat value increased. When the activity is determined by measuring the formation of N5-hydroxyornithine, the kcat value for the S257A enzyme is lower than that for the wild-type enzyme. The S257A mutation causes an increase in flexibility in two small loops, loop 253257, which is within interacting distance of NADP+ (including Ser257 and Gln256, which are able to form hydrogen bonds with NADP during MD simulations), and loop 453458, which resides 5 A from the FAD phosphate group. In contrast, loop 97105 (including Gln-102, which makes a hydrogen bond with FAD) presents reduced flexibility in the mutant enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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essential for virulence, validating this enzyme as a drug target