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Information on EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH)
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1.14.13.195 L-ornithine N5-monooxygenase (NADPH)IUBMB Comments
A flavoprotein (FAD). The enzyme is involved in biosynthesis of N5-hydroxy-L-ornithine, N5-formyl-N5-hydroxy-L-ornithine or N5-acetyl-N5-hydroxy-L-ornithine. These nonproteinogenic amino acids are building blocks of siderophores produced by some bacteria (e.g. Streptomyces coelicolor, Saccharopolyspora erythraea and Pseudomonas aeruginosa). The enzyme is specific for NADPH. cf. EC 1.14.13.196, L-ornithine N5-monooxygenase [NAD(P)H].
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Word Map
- 1.14.13.195
- flavin
- aspergillus
- fumigatus
-
flavin-dependent
-
pyoverdine
-
c4a-hydroperoxyflavin
- nadp+
- hydroxamate
-
hydroxamate-containing
-
flavin-containing
-
n-hydroxylating
-
non-ribosomal
-
half-reaction
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
Af-OMO, CchB, flavin-dependent monooxygenase, L-Orn N5-oxygenase, L-ornithine N5-hydroxylase, L-ornithine-Ndelta-oxygenase, monooxygenase EtcB, omega-amino acid monooxygenase, ornithine hydroxylase, ornithine N5-monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CchB
flavin-dependent monooxygenase
L-Orn N5-oxygenase
L-ornithine-Ndelta-oxygenase
PsbA
PvdA
SidA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O
binding of the hydroxylation target is not required to trigger reduction of flavin by NADPH, the reductive half-reaction proceeds in presence and absence of ornithine, reaction of O2 with FADH2 is accelerated 80fold by ornithine, ensuring coupling of NADPH and ornithine, C(4a)-hydroperoxyflavin intermediate, overview
-
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O
sequential kinetic mechanism for SidA. The reaction is initiated by binding of NADPH to SidA with the flavin in its oxidized form (FADox). The rate-limiting step in the reaction is the stereospecific transfer of the pro-R-hydride equivalent from NADPH to yield reduced flavin (FADred) and NADP+. The FADred-NADP+ complex reacts with molecular oxygen forming the C4a-hydroperoxyflavin (FADOOH). In this complex, NADP+ is essential for stabilization of the FADOOH. After ornithine (Orn) binding, hydroxylation occurs very quickly. The last step in the reaction is the release of products
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-ornithine,NADPH:oxygen oxidoreductase (N5-hydroxylating)
A flavoprotein (FAD). The enzyme is involved in biosynthesis of N5-hydroxy-L-ornithine, N5-formyl-N5-hydroxy-L-ornithine or N5-acetyl-N5-hydroxy-L-ornithine. These nonproteinogenic amino acids are building blocks of siderophores produced by some bacteria (e.g. Streptomyces coelicolor, Saccharopolyspora erythraea and Pseudomonas aeruginosa). The enzyme is specific for NADPH. cf. EC 1.14.13.196, L-ornithine N5-monooxygenase [NAD(P)H].
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CAS REGISTRY NUMBER
COMMENTARY
93229-65-3
-
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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 + NADH + H+ + O2
N5-hydroxy-L-ornithine + NAD+ + H2O
Q5SE95
-
-
-
?
L-lysine + NADPH + H+ + O2
N5-hydroxy-L-lysine + NADP+ + H2O
substrate with lower efficiency compared to L-ornithine
-
-
?
L-lysine + NADPH + H+ + O2
N5-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
Q5SE95
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
?
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
-
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
-
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
-
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
-
-
-
-
?
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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NATURAL SUBSTRATE
NATURAL 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
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
-
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
-
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
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
-
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
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
FAD or FMN, required, the reduction of FAD is ornithine-independent
NADPH
-
H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD
NADPH
-
no formation of N5-hydroxy-L-ornithine when NADH is utilized instead of NADPH as the reducing cosubstrate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chloride
-
mixed-type inhibitor with respect to ornithine, but a competitive inhibitor with respect to NADPH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-lysine
-
nonsubstrate activator stimulating NADPh oxidation 3.9fold at 2 mM causing H2O2 formation, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacteremia
The plasmid of neonatal meningitis Escherichia coli strain S88 (O45:K1:H7) is closely related to avian pathogenic E. coli plasmids and is associated with high level bacteremia in neonatal rat meningitis model.
Mycoses
Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics.
Starvation
Aspergillus flavus squalene synthase as an antifungal target: Expression, activity, and inhibition.
Tuberculosis
Mycobacterial siderophore: A review on chemistry and biology of siderophore and its potential as a target for tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
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
0.06
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.025
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.8
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
0.34
NADPH
Q5SE95
mutant S257A, hydroxylamine detection 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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.59
L-ornithine
-
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
1.06
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
0.88
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
0.11
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
0.59
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.53
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
0.15
L-ornithine
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
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
0.5
L-ornithine
-
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.5
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.45
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
0.12
NADPH
Q5SE95
mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
L-ornithine
-
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
0.62
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
0.042
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
0.042
L-ornithine
-
pH 7.5, 25°C, recombinant mutant N323A, 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
0.006
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
0.006
L-ornithine
-
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
15
NADPH
-
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
110
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
84.3
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
15
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
0.34
NADPH
Q5SE95
mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C
6
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
0.54
NADPH
Q5SE95
wild-type, hydroxylamine detection assay, pH 7.5, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
5-aminopentanoic acid
-
pH 8.0, 25°C, recombinant detagged enzyme
8.4
L-2,4-diaminobutyrate
-
pH 8.0, 25°C, recombinant detagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
pI values, calculated for the truncated enzyme fragments, overview
additional information
-
pI values, calculated for the truncated enzyme fragments, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme anchors in the inner membrane with its N-terminus, while the bulk of the enzyme is located in the cytosol, the transmembrane region overlaps the FAd binding site, membrane-association determinants of PvdA and analysis of membrane topology, overview
-
brenda
-
a substantial amount of the enzyme is located in the membrane fraction. It is mainly clustered at the old cell pole of bacteria, indicating a polar segregation of the protein
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PVDA_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
443
0
49478
Swiss-Prot
-
A0A2V0QZD1_PSESF
458
0
51185
TrEMBL
-
A0A6L5BR58_9PSED
445
0
49926
TrEMBL
-
A0A221JW85_9RHOB
425
0
47228
TrEMBL
-
A0A346B6K0_9BURK
459
0
51268
TrEMBL
-
SIDA_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
501
0
56877
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer or pentamer
-
x * 51000, recombinant His-tagged enzyme, SDS-PAGE
additional information
additional information
immunochemical peptide mapping, molecular weights calculated for the truncated enzyme fragments, overview
additional information
-
immunochemical peptide mapping, molecular weights calculated for the truncated enzyme fragments, overview
additional information
-
PvdA secondary structure and transmembrane region, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme mutant N323A complexed with NADP+ and ornithine, hanging drop vapor diffusion method and microseeding, mixing of mixing of 8 mg/ml SidA N323A mutant protein, preincubated with 1 mM NADP+ and 100 mM ornithine, with an equal volume of reservoir solution containing 0.1 M HEPES, pH 6.6, 1.86 M ammonium sulfate, and 1% v/v dioxane, X-ray diffraction structure determination and analysis at 2.10 A resolution
crystal structures of the enzyme with FAD in oxidized (1.9 A resolution) and reduced (3.03 A resolution) states. Crystals are obtained through the hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2(DE3) by nickel affinity chromatography, the tag is cleaved off by thrombin
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by affinity chromatography, proteolytic tag removal
recombinant N-terminally His-tagged full-length and truncated wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography
recombinant N-terminally thioredoxin-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of PvdA-PhoA fusion protein mutants in Escherichia coli strain LMG194
-
gene cchB, overexpression of N-terminally thioredoxin-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene psbA, DNA and amino acid sequence determination and analysis, monocistronic gene
gene pvdA, expression of His-tagged enzyme in Escherichia coli strain Rosetta2(DE3)
-
gene sidA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)-T1
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons, promoter activity analysis during cell growth. Recombinant expression of N-terminally His-tagged full-length and truncated wild-type and mutant enzymes in Escherichia coli strain M15
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
-
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
-
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
-
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
-
PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is induced by iron
the psbA expression is negatively controlled by iron
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 aeruginosa (Q51548), Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas syringae, Ralstonia solanacearum
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
Meneely, K.M.; Barr, E.W.; Bollinger, J.M. Jr.; Lamb, A.L.
Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction
Biochemistry
48
4371-4376
2009
Pseudomonas aeruginosa
brenda
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
J. Bacteriol.
182
6233-6238
2000
Pseudomonas sp. (Q9F8X0), Pseudomonas sp. B10 (Q9F8X0)
brenda
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.
188
7205-7210
2006
Pseudomonas aeruginosa
brenda
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
brenda
Pohlmann, V.; Marahiel, M.A.
delta-Amino group hydroxylation of L-ornithine during coelichelin biosynthesis
Org. Biomol. Chem.
6
1843-1848
2008
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
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
brenda
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
brenda
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.
14
1982-1994
2012
Pseudomonas aeruginosa
brenda
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
brenda
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
brenda
Badieyan, S.; Bach, R.; Sobrado, P.
Mechanism of N-hydroxylation catalyzed by flavin-dependent monooxygenases
J. Org. Chem.
80
2139-2147
2015
Aspergillus fumigatus (E9QYP0), Aspergillus fumigatus Af293 (E9QYP0)
brenda
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
brenda
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