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L-lysine + NADPH + H+ + O2
L-lysine N6-oxide + NADP+ + H2O
-
-
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
L-ornithine + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
additional information
?
-
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
substrate with lower efficiency compared to L-ornithine
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
substrate with lower efficiency compared to L-ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
Q5SE95
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
hydroxylation of the primary amine of ornithine in the initial step of the biosynthesis of siderophore pyoverdin
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
hydroxylation of the primary amine of ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
no activity with D-ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
PvdA is highly specific for both substrate and coenzyme, PvdA/FAD forms a ternary complex with NADPH and ornithine for catalysis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
one of the initial enzymes in the biosynthetic pathway of pyoverdine I the major siderophore produced by Pseudomonas aeruginosa PAO1 to import iron
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
the enzyme contains the FATGY signature in the putative substrate binding pocket
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
the enzyme contains the FATGY signature in the putative substrate binding pocket
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
the enzyme is involved in biosynthesis of N5-acetyl-N5-hydroxy-L-ornithine, a building block of the hydroxamate-type siderophore erythrochelin
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
absolutely specific for L-ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
absolutely specific for L-ornithine
-
-
?
additional information
?
-
Q5SE95
when the enzyme is reduced with NADPH and reacts with molecular oxygen, a C4a-hydroperoxyflavin intermediate is observed. When the enzyme is reduced with NADH, the intermediate is 2fold less stable. Steady-state kinetic isotope effect values for NADPH and NADH are 3 and 2 , respectively, due to differences in the rate of flavin reduction by these coenzymes. NADP+, and not NAD+, protects the enzyme from proteolysis, suggesting that it induces conformational changes upon binding
-
-
?
additional information
?
-
-
when the enzyme is reduced with NADPH and reacts with molecular oxygen, a C4a-hydroperoxyflavin intermediate is observed. When the enzyme is reduced with NADH, the intermediate is 2fold less stable. Steady-state kinetic isotope effect values for NADPH and NADH are 3 and 2 , respectively, due to differences in the rate of flavin reduction by these coenzymes. NADP+, and not NAD+, protects the enzyme from proteolysis, suggesting that it induces conformational changes upon binding
-
-
?
additional information
?
-
-
PvdA is the ornithine hydroxylase, which performs the first enzymatic step in preparation of hydroxamate siderophore derivatives, pyoverdin is the hydroxamate siderophore produced by the opportunistic pathogen Pseudomonas aeruginosa under the iron-limiting conditions of the human host, overview. Poor activity with DL-2,3-diaminopropionic acid and D-ornithine, no activity with L-norleucine, 5-aminopentanoic acid, DL-2,4-diaminobutyric acid, and 1,4-diaminobutane, and no activity with NADH as cofactor, substrate specificity, overview
-
-
?
additional information
?
-
-
extending the side chain by one methylene group to L-lysine results in significant NADPH oxidation without formation of the hydroxylated product, indicating that the reaction is uncoupled
-
-
?
additional information
?
-
-
H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD
-
-
?
additional information
?
-
-
the NADPH oxidase activity of the enzyme is tightly coupled to hydroxylamine formation
-
-
?
additional information
?
-
-
no activity with D-ornithine, N5-formylornithine, L-lysine, L-glutamate, L-glutamine, L-valine, and the tetrapeptide D-Orn-D-Thr-L-Orn-D-Orn, the enzyme performs NADPH oxidation with formation of H2O2, substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with D-ornithine, N5-formylornithine, L-lysine, L-glutamate, L-glutamine, L-valine, and the tetrapeptide D-Orn-D-Thr-L-Orn-D-Orn, the enzyme performs NADPH oxidation with formation of H2O2, substrate specificity, overview
-
-
?
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L-lysine + NADPH + H+ + O2
L-lysine N6-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
additional information
?
-
-
PvdA is the ornithine hydroxylase, which performs the first enzymatic step in preparation of hydroxamate siderophore derivatives, pyoverdin is the hydroxamate siderophore produced by the opportunistic pathogen Pseudomonas aeruginosa under the iron-limiting conditions of the human host, overview. Poor activity with DL-2,3-diaminopropionic acid and D-ornithine, no activity with L-norleucine, 5-aminopentanoic acid, DL-2,4-diaminobutyric acid, and 1,4-diaminobutane, and no activity with NADH as cofactor, substrate specificity, overview
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
hydroxylation of the primary amine of ornithine in the initial step of the biosynthesis of siderophore pyoverdin
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
one of the initial enzymes in the biosynthetic pathway of pyoverdine I the major siderophore produced by Pseudomonas aeruginosa PAO1 to import iron
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
the enzyme is involved in biosynthesis of N5-acetyl-N5-hydroxy-L-ornithine, a building block of the hydroxamate-type siderophore erythrochelin
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0219
FAD
-
pH 8.0, 25°C, recombinant detagged enzyme
0.1
NADH
Q5SE95
pH 7.5, 15°C
additional information
additional information
-
0.058
L-ornithine
-
pH 8.0, 25°C, recombinant detagged enzyme
0.286
L-ornithine
-
pH 8.0, 25°C
1
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
1.1
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
12
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
15
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
16
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
18
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
18
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
21
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.007
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.01
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
0.012
NADPH
Q5SE95
pH 7.5, 15°C
0.014
NADPH
Q5SE95
mutant S257A, O2 consumption assay, pH 7.5, 25°C
0.017
NADPH
Q5SE95
wild-type, O2 consumption assay, pH 7.5, 25°C
0.025
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.06
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.16
NADPH
-
pH 8.0, 25°C, recombinant detagged enzyme
0.34
NADPH
Q5SE95
mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C
0.8
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic mechanism of oxidative and reductive half-reactions, stopped-flow kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis, overview
-
additional information
additional information
Pre-steady-state kinetics and steady-state kinetics
-
additional information
additional information
-
Pre-steady-state kinetics and steady-state kinetics
-
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0.73
NADH
Q5SE95
pH 7.5, 15°C
0.11
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
0.15
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.327
L-ornithine
-
pH 8.0, 25°C
0.5
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.53
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
0.59
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
0.88
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
1.06
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
0.12
NADPH
Q5SE95
mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C
0.45
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
0.6
NADPH
Q5SE95
pH 7.5, 15°C
0.6
NADPH
Q5SE95
wild-type, O2 consumption assay, pH 7.5, 25°C
0.85
NADPH
Q5SE95
mutant S257A, O2 consumption assay, pH 7.5, 25°C
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10
NADH
Q5SE95
pH 7.5, 15°C
0.006
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.006
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
0.033
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.033
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
0.042
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
0.042
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
1.14
L-ornithine
-
pH 8.0, 25°C
0.34
NADPH
Q5SE95
mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C
0.54
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
6
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
14
NADPH
Q5SE95
wild-type, O2 consumption assay, pH 7.5, 25°C
15
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
40
NADPH
Q5SE95
mutant S257A, O2 consumption assay, pH 7.5, 25°C
50
NADPH
Q5SE95
pH 7.5, 15°C
84.3
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
110
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
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metabolism
-
the enzyme catalyzes the first committed step in hydroxamate siderophore biosynthesis, e.g. N',N'',N'''-triacetylfusarinine C, i.e. TAF, and ferricrocin, which are essential for cell growth, overview
metabolism
-
the enzyme catalyzes the initial step of the biosynthesis of siderophore pyoverdin
physiological function
-
L-ornithiine N5-oxygenase is indispensable for deferriderrichrysin biosynthesis
physiological function
-
the enzyme catalyzes the first committed step in hydroxamate siderophore biosynthesis, e.g. N',N'',N'''-triacetylfusarinine C, i.e. TAF, and ferricrocin, which are essential for cell growth, overview. The enzymeis required for secretion of the siderophores and for the virulence of the organism in mice
physiological function
-
the enzyme is involved in pyoverdine siderophore biosynthesis, pyoverdine is required for acquiration of the essential iron from the host
physiological function
-
the enzyme is involved in the siderophore system, essential for viability, overview
physiological function
-
the enzyme is required for synthesis of the nonproteinogenic amino acids N5-hydroxyornithine and N5-hydroxyformylornithine, that are required for iron assembly by the organism
physiological function
Q5SE95
enzyme is essential for virulence
physiological function
-
the enzyme is required for synthesis of the nonproteinogenic amino acids N5-hydroxyornithine and N5-hydroxyformylornithine, that are required for iron assembly by the organism
-
additional information
residue Asn323 interacts with the enzyme and also interacts with NADPH by forming a hydrogen bond with the nicotinamide ribose, residue K107 is important for catalytic activity. Asn323 thus facilitates ornithine binding at the expense of hindering flavin reduction
additional information
-
residue Asn323 interacts with the enzyme and also interacts with NADPH by forming a hydrogen bond with the nicotinamide ribose, residue K107 is important for catalytic activity. Asn323 thus facilitates ornithine binding at the expense of hindering flavin reduction
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K107A
site-directed mutagenesis, inactive mutant
N293A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
N323A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type, and to increased rate constant for flavin reduction by NADPH by 18fold
S257A
Q5SE95
the interaction between residue Ser257 and NADP(H) is essential for stabilization of the C4a-hydroperoxyflavin intermediate. Ser257 may function as a pivot point, allowing the nicotinamide of NADP+ to slide into position for stabilization of the C4a-hydroperoxyflavin
S469A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
additional information
construction of diverse inactive truncation mutants, overview
additional information
-
construction of diverse inactive truncation mutants, overview
additional information
-
construction of PvdA-PhoA fusion protein mutantsa nd of a pvdA deletion mutant strain
additional information
a PsbA-defective mutant B10CA1 is fully complemented by addition of L-ornithine N5-oxide, the mutant strain shows impaired synthesis of fluorescent pigment and hydroxamate nitrogen in iron-poor medium, as well as defective biosynthesis of both forms of pseudobactin and salicylate-based siderophores, Fe3+ transfer is impaired, phenotype, overview
additional information
-
a PsbA-defective mutant B10CA1 is fully complemented by addition of L-ornithine N5-oxide, the mutant strain shows impaired synthesis of fluorescent pigment and hydroxamate nitrogen in iron-poor medium, as well as defective biosynthesis of both forms of pseudobactin and salicylate-based siderophores, Fe3+ transfer is impaired, phenotype, overview
-
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Putignani, L.; Ambrosi, C.; Ascenzi, P.; Visca, P.
Expression of L-ornithine Ndelta-oxygenase (PvdA) in fluorescent Pseudomonas species: an immunochemical and in silico study
Biochem. Biophys. Res. Commun.
313
245-257
2004
Burkholderia cepacia, Pseudomonas putida, Pseudomonas fluorescens, Ralstonia solanacearum, Pseudomonas syringae, Pseudomonas aeruginosa (Q51548), Pseudomonas aeruginosa
brenda
Meneely, K.M.; Lamb, A.L.
Biochemical characterization of a flavin adenine dinculeotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism
Biochemistry
46
11930-11937
2007
Pseudomonas aeruginosa
brenda
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Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction
Biochemistry
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2009
Pseudomonas aeruginosa
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Ambrosi, C.; Leoni, L.; Putignani, L.; Orsi, N.; Visca, P.
Pseudobactin biogenesis, in the plant growth-promoting rhizobacterium Pseudomonas strain B10: Identification and functional analysis of the L-ornithine N5-oxygenase (psbA) gene
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Pseudomonas sp. (Q9F8X0), Pseudomonas sp. B10 (Q9F8X0)
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Ge, L.; Seah, S.Y.K.
Heterologous expression, purification, and characterization of an L-ornithine N5-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa
J. Bacteriol.
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7205-7210
2006
Pseudomonas aeruginosa
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Imperi, F.; Putignani, L.; Tiburzi, F.; Ambrosi, C.; Cipollone, R.; Ascenzi, P.; Visca, P.
Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa
Microbiology
154
2804-2813
2008
Pseudomonas aeruginosa
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Pohlmann, V.; Marahiel, M.A.
delta-Amino group hydroxylation of L-ornithine during coelichelin biosynthesis
Org. Biomol. Chem.
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1843-1848
2008
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
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Robbel, L.; Helmetag, V.; Knappe, T.A.; Marahiel, M.A.
Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin
Biochemistry
50
6073-6080
2011
Saccharopolyspora erythraea
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Romero, E.; Fedkenheuer, M.; Chocklett, S,W.; Qi, J.; Oppenheimer, M.; Sobrado, P.
Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase
Biochim. Biophys. Acta
1824
850-857
2012
Aspergillus fumigatus (Q5SE95), Aspergillus fumigatus
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Guillon, L.; El Mecherki, M.; Altenburger, S.; Graumann, P.L.; Schalk, I.J.
High cellular organization of pyoverdine biosynthesis in Pseudomonas aeruginosa: clustering of PvdA at the old cell pole
Environ. Microbiol.
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2012
Pseudomonas aeruginosa
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Frederick, R.E.; Mayfield, J.A.; DuBois, J.L.
Regulated O2 activation in flavin-dependent monooxygenases
J. Am. Chem. Soc.
133
12338-12341
2011
Aspergillus fumigatus
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Olucha, J.; Meneely, K.M.; Chilton, A.S.; Lamb, A.L.
Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine hydroxylase from Pseudomonas aeruginosa
J. Biol. Chem.
286
31789-31798
2011
Pseudomonas aeruginosa (Q51548), Pseudomonas aeruginosa
brenda
Shirey, C.; Badieyan, S.; Sobrado, P.
Role of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA
J. Biol. Chem.
288
32440-32448
2013
Aspergillus fumigatus (Q5SE95), Aspergillus fumigatus
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Badieyan, S.; Bach, R.; Sobrado, P.
Mechanism of N-hydroxylation catalyzed by flavin-dependent monooxygenases
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2139-2147
2015
Aspergillus fumigatus (E9QYP0), Aspergillus fumigatus Af293 (E9QYP0)
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Robinson, R.; Qureshi, I.A.; Klancher, C.A.; Rodriguez, P.J.; Tanner, J.J.; Sobrado, P.
Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase
Arch. Biochem. Biophys.
585
25-31
2015
Aspergillus fumigatus (E9QYP0), Aspergillus fumigatus
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