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Enzyme Nomenclature
Information on EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH)
for references in articles please use BRENDA:EC1.14.13.195
Word Map on EC 1.14.13.195
- 1.14.13.195
- flavin
- fumigatus
- aeruginosa
-
pyoverdine
-
flavin-dependent
- nadp+
- hydroxamate
-
c4a-hydroperoxyflavin
-
hydroxamate-containing
-
n-hydroxylating
-
half-reaction
-
flavin-containing
-
ferrichrome
- p-hydroxybenzoate
-
iron-deficient
-
iron-limiting
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.13.195
-
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RECOMMENDED NAME
GeneOntology No.
L-ornithine N5-monooxygenase (NADPH)
-
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
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
metabolism
-
the enzyme catalyzes the initial step of the biosynthesis of siderophore pyoverdin
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
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
-
L-ornithiine N5-oxygenase is indispensable for deferriderrichrysin biosynthesis
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
-
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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
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
no activity with D-ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + 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
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
the enzyme contains the FATGY signature in the putative substrate binding pocket
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
the enzyme contains the FATGY signature in the putative substrate binding pocket
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
absolutely specific for L-ornithine
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + 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
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
-
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
-
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 + NADPH + 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 + NADPH + H2O
-
hydroxylation of the primary amine of 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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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 + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADPH + H2O
-
hydroxylation of the primary amine of ornithine in the initial step of the biosynthesis of siderophore pyoverdin
-
-
?
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
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q51548
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
Q9F8X0
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
first step in pyoverdine biosynthesis
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
E9QYP0
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
-
?
L-ornithine + NADPH + H+ + O2
N5-hydroxy-L-ornithine + NADP+ + H2O
E9QYP0
-
-
-
?
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
-
the enzyme is involved in biosynthesis of N5-acetyl-N5-hydroxy-L-ornithine, a building block of the hydroxamate-type siderophore erythrochelin
-
-
?
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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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INHIBITORS
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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; 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
0.025
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
-
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
-
Michaelis-Menten 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
0.11
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
0.53
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
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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; 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; 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; 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; pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
15
NADPH
-
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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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
-
-
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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer or pentamer
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x * 51000, recombinant His-tagged enzyme, SDS-PAGE
additional information
additional information
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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
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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
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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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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
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recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by affinity chromatography, proteolytic tag removal
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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
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gene cchB, overexpression of N-terminally thioredoxin-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene psbA, DNA and amino acid sequence determination and analysis, monocistronic gene
Q9F8X0
gene pvdA, expression of His-tagged enzyme in Escherichia coli strain Rosetta2(DE3)
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gene sidA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)-T1
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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
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PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
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PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
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PvdA, DNA and amino acid sequence determination and analysis, sequence comparisons
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N293A
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site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
N323A
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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
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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
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site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
additional information
additional information
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construction of diverse inactive truncation mutants, overview
additional information
construction of diverse inactive truncation mutants, overview
additional information
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construction of PvdA-PhoA fusion protein mutantsa nd of a pvdA deletion mutant strain
additional information
Q9F8X0
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.195)
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