BRENDA - Enzyme Database show
show all sequences of 1.14.13.195

Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase

Robinson, R.; Qureshi, I.A.; Klancher, C.A.; Rodriguez, P.J.; Tanner, J.J.; Sobrado, P.; Arch. Biochem. Biophys. 585, 25-31 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene sidA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)-T1
Aspergillus fumigatus
Crystallization (Commentary)
Crystallization
Organism
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
Aspergillus fumigatus
Engineering
Amino acid exchange
Commentary
Organism
K107A
site-directed mutagenesis, inactive mutant
Aspergillus fumigatus
N293A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
Aspergillus fumigatus
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
Aspergillus fumigatus
S469A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
Aspergillus fumigatus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Pre-steady-state kinetics and steady-state kinetics
Aspergillus fumigatus
0.007
-
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
0.01
-
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
0.025
-
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
0.06
-
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
1
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
Aspergillus fumigatus
1.1
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
12
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
Aspergillus fumigatus
15
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
16
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
Aspergillus fumigatus
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
Aspergillus fumigatus
21
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-ornithine + NADPH + H+ + O2
Aspergillus fumigatus
-
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus fumigatus
E9QYP0
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by affinity chromatography, proteolytic tag removal
Aspergillus fumigatus
Reaction
Reaction
Commentary
Organism
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
Aspergillus fumigatus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-ornithine + NADPH + H+ + O2
-
744163
Aspergillus fumigatus
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Aspergillus fumigatus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.11
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
Aspergillus fumigatus
0.15
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
0.5
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
Aspergillus fumigatus
0.53
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
Aspergillus fumigatus
0.59
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
0.62
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
Aspergillus fumigatus
0.88
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
1.06
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Aspergillus fumigatus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Aspergillus fumigatus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene sidA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)-T1
Aspergillus fumigatus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Aspergillus fumigatus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Aspergillus fumigatus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K107A
site-directed mutagenesis, inactive mutant
Aspergillus fumigatus
N293A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
Aspergillus fumigatus
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
Aspergillus fumigatus
S469A
site-directed mutagenesis, the mutation leads to highly increased Km for L-ornithine compared to the wild-type
Aspergillus fumigatus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Pre-steady-state kinetics and steady-state kinetics
Aspergillus fumigatus
0.007
-
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
0.01
-
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
0.025
-
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
0.06
-
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
1
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
Aspergillus fumigatus
1.1
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
12
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
Aspergillus fumigatus
15
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
16
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
Aspergillus fumigatus
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
Aspergillus fumigatus
21
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-ornithine + NADPH + H+ + O2
Aspergillus fumigatus
-
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by affinity chromatography, proteolytic tag removal
Aspergillus fumigatus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-ornithine + NADPH + H+ + O2
-
744163
Aspergillus fumigatus
N5-hydroxy-L-ornithine + NADP+ + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Aspergillus fumigatus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.11
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay
Aspergillus fumigatus
0.15
-
L-ornithine
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
0.5
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay
Aspergillus fumigatus
0.53
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay
Aspergillus fumigatus
0.59
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
0.62
-
L-ornithine
pH 7.5, 25°C, recombinant wild-type enzyme, ornithine hydroxylation assay
Aspergillus fumigatus
0.88
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
1.06
-
L-ornithine
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Aspergillus fumigatus
General Information
General Information
Commentary
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
Aspergillus fumigatus
General Information (protein specific)
General Information
Commentary
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
Aspergillus fumigatus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
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
Aspergillus fumigatus
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
Aspergillus fumigatus
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
Aspergillus fumigatus
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
Aspergillus fumigatus
6
-
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
15
-
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
84.3
-
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
110
-
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
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
Aspergillus fumigatus
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
Aspergillus fumigatus
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
Aspergillus fumigatus
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
Aspergillus fumigatus
6
-
NADPH
pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay
Aspergillus fumigatus
15
-
NADPH
pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay
Aspergillus fumigatus
84.3
-
NADPH
pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay
Aspergillus fumigatus
110
-
NADPH
pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay
Aspergillus fumigatus
Other publictions for EC 1.14.13.195
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743137
Badieyan
Mechanism of N-hydroxylation ...
Aspergillus fumigatus, Aspergillus fumigatus Af293
J. Org. Chem.
80
2139-2147
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
744163
Robinson
Contribution to catalysis of ...
Aspergillus fumigatus
Arch. Biochem. Biophys.
585
25-31
2015
-
-
1
1
4
-
-
12
-
-
-
1
-
2
-
-
1
1
-
-
-
-
1
-
1
-
-
8
1
-
-
1
-
-
-
-
-
1
1
1
4
-
-
-
-
12
-
-
-
1
-
-
-
1
-
-
-
-
1
-
1
-
-
8
1
-
-
-
-
1
1
-
8
8
725540
Shirey
Role of Ser-257 in the sliding ...
Aspergillus fumigatus
J. Biol. Chem.
288
32440-32448
2013
-
-
1
-
1
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
4
4
724451
Romero
Dual role of NADP(H) in the re ...
Aspergillus fumigatus
Biochim. Biophys. Acta
1824
850-857
2012
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
1
1
-
2
2
724860
Guillon
High cellular organization of ...
Pseudomonas aeruginosa
Environ. Microbiol.
14
1982-1994
2012
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714263
Robbel
Consecutive enzymatic modifica ...
Saccharopolyspora erythraea
Biochemistry
50
6073-6080
2011
-
-
1
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
1
-
-
1
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
2
-
1
-
-
1
1
-
-
-
-
-
-
-
1
1
725195
Frederick
Regulated O2 activation in fla ...
Aspergillus fumigatus
J. Am. Chem. Soc.
133
12338-12341
2011
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
725440
Olucha
Two structures of an N-hydroxy ...
Pseudomonas aeruginosa
J. Biol. Chem.
286
31789-31798
2011
-
-
-
1
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
702303
Meneely
Kinetic mechanism of ornithine ...
Pseudomonas aeruginosa
Biochemistry
48
4371-4376
2009
-
-
-
-
-
-
-
1
-
-
-
1
-
2
-
1
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
705555
Imperi
Membrane-association determina ...
Pseudomonas aeruginosa
Microbiology
154
2804-2813
2008
-
-
1
-
1
-
-
-
1
-
-
-
-
4
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
706031
Pohlmann
delta-Amino group hydroxylatio ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Org. Biomol. Chem.
6
1843-1848
2008
-
-
1
-
-
-
-
1
-
-
-
2
-
42
-
1
1
-
-
-
-
-
6
-
1
-
-
-
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
-
-
2
-
-
1
1
-
-
-
-
6
-
1
-
-
-
1
1
-
-
-
1
1
-
-
-
702210
Meneely
Biochemical characterization o ...
Pseudomonas aeruginosa
Biochemistry
46
11930-11937
2007
-
-
-
-
-
-
3
1
1
-
-
3
-
5
-
1
-
-
-
-
2
-
5
1
-
-
-
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
3
-
1
1
-
-
3
-
-
1
-
-
-
2
-
5
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
704269
Ge
Heterologous expression, purif ...
Pseudomonas aeruginosa
J. Bacteriol.
188
7205-7210
2006
2
-
1
-
-
-
3
4
-
-
2
1
-
1
-
1
1
-
-
-
1
-
3
1
1
-
-
-
1
1
-
3
4
-
-
2
-
1
3
-
-
-
-
3
4
4
-
-
2
1
-
-
1
1
-
-
1
-
3
1
1
-
-
-
1
1
-
-
-
1
1
-
-
-
702009
Putignani
Expression of L-ornithine Ndel ...
Burkholderia cepacia, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas syringae, Ralstonia solanacearum
Biochem. Biophys. Res. Commun.
313
245-257
2004
-
-
6
-
1
-
-
-
-
-
-
6
-
15
-
6
1
-
-
-
-
-
12
1
-
-
-
-
-
-
-
12
-
1
-
-
-
6
12
-
1
-
-
-
-
-
-
-
-
6
-
-
6
1
-
-
-
-
12
1
-
-
-
-
-
-
-
1
5
-
-
5
-
-
704262
Ambrosi
Pseudobactin biogenesis, in th ...
Pseudomonas sp., Pseudomonas sp. B10
J. Bacteriol.
182
6233-6238
2000
-
-
1
-
1
-
-
-
-
1
-
2
-
2
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-