BRENDA - Enzyme Database show
show all sequences of 1.14.13.195

Biochemical characterization of a flavin adenine dinculeotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism

Meneely, K.M.; Lamb, A.L.; Biochemistry 46, 11930-11937 (2007)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
4-chloromercuribenzoate
a mixed inhibitor with respect to ornithine
Pseudomonas aeruginosa
chloride
mixed-type inhibitor with respect to ornithine, but a competitive inhibitor with respect to NADPH
Pseudomonas aeruginosa
L-lysine
mixed-type inhibition
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Pseudomonas aeruginosa
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Pseudomonas aeruginosa
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-lysine + NADPH + H+ + O2
Pseudomonas aeruginosa
-
L-lysine N6-oxide + NADP+ + H2O
-
-
?
L-ornithine + NADPH + H+ + O2
Pseudomonas aeruginosa
-
L-ornithine N5-oxide + NADP+ + H2O
-
-
?
additional information
Pseudomonas aeruginosa
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
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
flavoprotein
-
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.321
-
L-ornithine hydroxylation
Pseudomonas aeruginosa
0.534
-
NADPH oxidation
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine + NADPH + H+ + O2
-
702210
Pseudomonas aeruginosa
L-lysine N6-oxide + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
-
702210
Pseudomonas aeruginosa
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
PvdA is highly specific for both substrate and coenzyme, PvdA/FAD forms a ternary complex with NADPH and ornithine for catalysis
702210
Pseudomonas aeruginosa
L-ornithine N5-oxide + 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
702210
Pseudomonas aeruginosa
?
-
-
-
-
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
702210
Pseudomonas aeruginosa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
-
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Pseudomonas aeruginosa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
10
-
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Pseudomonas aeruginosa
additional information
no activity with NADH as cofactor
Pseudomonas aeruginosa
NADPH
dependent on
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Pseudomonas aeruginosa
additional information
no activity with NADH as cofactor
Pseudomonas aeruginosa
NADPH
dependent on
Pseudomonas aeruginosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-chloromercuribenzoate
a mixed inhibitor with respect to ornithine
Pseudomonas aeruginosa
chloride
mixed-type inhibitor with respect to ornithine, but a competitive inhibitor with respect to NADPH
Pseudomonas aeruginosa
L-lysine
mixed-type inhibition
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Pseudomonas aeruginosa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Pseudomonas aeruginosa
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-lysine + NADPH + H+ + O2
Pseudomonas aeruginosa
-
L-lysine N6-oxide + NADP+ + H2O
-
-
?
L-ornithine + NADPH + H+ + O2
Pseudomonas aeruginosa
-
L-ornithine N5-oxide + NADP+ + H2O
-
-
?
additional information
Pseudomonas aeruginosa
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
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
flavoprotein
-
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.321
-
L-ornithine hydroxylation
Pseudomonas aeruginosa
0.534
-
NADPH oxidation
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine + NADPH + H+ + O2
-
702210
Pseudomonas aeruginosa
L-lysine N6-oxide + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
-
702210
Pseudomonas aeruginosa
L-ornithine N5-oxide + NADP+ + H2O
-
-
-
?
L-ornithine + NADPH + H+ + O2
PvdA is highly specific for both substrate and coenzyme, PvdA/FAD forms a ternary complex with NADPH and ornithine for catalysis
702210
Pseudomonas aeruginosa
L-ornithine N5-oxide + 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
702210
Pseudomonas aeruginosa
?
-
-
-
-
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
702210
Pseudomonas aeruginosa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
-
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Pseudomonas aeruginosa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
10
-
Pseudomonas aeruginosa
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
-
-