BRENDA - Enzyme Database
show all sequences of 1.2.1.65

Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway

Jia, B.; Jia, X.; Hyun Kim, K.; Ji Pu, Z.; Kang, M.S.; Ok Jeon, C.; Sci. Rep. 7, 43489 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
Alteromonas naphthalenivorans
Engineering
Amino acid exchange
Commentary
Organism
E175A
site-directed mutagenesis, the apparent Km value of the mutant enzyme to NAD+ is increased by about 2times and the kcat/Km toward the cofactor decreased by 4times. The Km value of the mutant toward salicylaldehyde also increases and the catalytic efficiency decreases by 6times compared to the wild-type enzyme
Alteromonas naphthalenivorans
additional information
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis
Alteromonas naphthalenivorans
N149A
site-directed mutagenesis, the catalyic efficiency of the mutant is decreased compared to the wild-type enzyme
Alteromonas naphthalenivorans
V153A
site-directed mutagenesis, the mutation has no significant effect on the kinetic parameters for either NAD+ or salicylaldehyde compared to the wild-type enzyme
Alteromonas naphthalenivorans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Salicylaldehyde
substrate inhibition
Alteromonas naphthalenivorans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
bisubstrate Michaelis-Menten kinetics
Alteromonas naphthalenivorans
0.0038
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.0046
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.0095
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.0151
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
0.0395
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.0449
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.0523
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.1056
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
160000
-
recombinant His-tagged enzyme, gel filtration
Alteromonas naphthalenivorans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
salicylaldehyde + NAD+ + H2O
Alteromonas naphthalenivorans
-
salicylate + NADH + 2 H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Alteromonas naphthalenivorans
F5Z5S7
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Alteromonas naphthalenivorans
Reaction
Reaction
Commentary
Organism
salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+
catalytic mechanism, overview
Alteromonas naphthalenivorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
salicylaldehyde + NAD+ + H2O
-
743833
Alteromonas naphthalenivorans
salicylate + NADH + 2 H+
-
-
-
?
salicylaldehyde + NAD+ + H2O
amino acids Asn149 and Glu250 may bind salicylaldehyde
743833
Alteromonas naphthalenivorans
salicylate + NADH + 2 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotrimer
3 * 53000, recombinant His-tagged enzyme, SDS-PAGE
Alteromonas naphthalenivorans
More
substrate binding induces a conformational change. SALDan three-dimensional homology modeling using the crystal structures of SALDpp, PDB ID 4JZ6, and other aldehyde dehydrogenases, PDB IDs 4FR8, 4O6R, 4NMK, 2O2P, and 3PQA, as model structures
Alteromonas naphthalenivorans
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
35
high activity within this range
Alteromonas naphthalenivorans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
82.2
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
100.4
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
123.6
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
153.5
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
157.6
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
208.8
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
234.3
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
254.5
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Alteromonas naphthalenivorans
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
9
high activity within this range
Alteromonas naphthalenivorans
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release
Alteromonas naphthalenivorans
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.3787
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.4283
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.4467
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.4616
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
Cloned(Commentary) (protein specific)
Commentary
Organism
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
Alteromonas naphthalenivorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release
Alteromonas naphthalenivorans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E175A
site-directed mutagenesis, the apparent Km value of the mutant enzyme to NAD+ is increased by about 2times and the kcat/Km toward the cofactor decreased by 4times. The Km value of the mutant toward salicylaldehyde also increases and the catalytic efficiency decreases by 6times compared to the wild-type enzyme
Alteromonas naphthalenivorans
additional information
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis
Alteromonas naphthalenivorans
N149A
site-directed mutagenesis, the catalyic efficiency of the mutant is decreased compared to the wild-type enzyme
Alteromonas naphthalenivorans
V153A
site-directed mutagenesis, the mutation has no significant effect on the kinetic parameters for either NAD+ or salicylaldehyde compared to the wild-type enzyme
Alteromonas naphthalenivorans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Salicylaldehyde
substrate inhibition
Alteromonas naphthalenivorans
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.3787
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.4283
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.4467
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.4616
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
bisubstrate Michaelis-Menten kinetics
Alteromonas naphthalenivorans
0.0038
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.0046
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.0095
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
0.0151
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
0.0395
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
0.0449
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.0523
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
0.1056
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
160000
-
recombinant His-tagged enzyme, gel filtration
Alteromonas naphthalenivorans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
salicylaldehyde + NAD+ + H2O
Alteromonas naphthalenivorans
-
salicylate + NADH + 2 H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Alteromonas naphthalenivorans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
salicylaldehyde + NAD+ + H2O
-
743833
Alteromonas naphthalenivorans
salicylate + NADH + 2 H+
-
-
-
?
salicylaldehyde + NAD+ + H2O
amino acids Asn149 and Glu250 may bind salicylaldehyde
743833
Alteromonas naphthalenivorans
salicylate + NADH + 2 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotrimer
3 * 53000, recombinant His-tagged enzyme, SDS-PAGE
Alteromonas naphthalenivorans
More
substrate binding induces a conformational change. SALDan three-dimensional homology modeling using the crystal structures of SALDpp, PDB ID 4JZ6, and other aldehyde dehydrogenases, PDB IDs 4FR8, 4O6R, 4NMK, 2O2P, and 3PQA, as model structures
Alteromonas naphthalenivorans
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
35
high activity within this range
Alteromonas naphthalenivorans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
82.2
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
100.4
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
123.6
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
153.5
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
157.6
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
208.8
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
234.3
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
254.5
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Alteromonas naphthalenivorans
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
9
high activity within this range
Alteromonas naphthalenivorans
Expression
Organism
Commentary
Expression
Alteromonas naphthalenivorans
SALD from Alteromonas naphthalenivorans (SALDan) is specifically upregulated in response to naphthalene
up
General Information
General Information
Commentary
Organism
evolution
network and phylogenetic analyses indicated that salicylaldehyde dehydrogenases (SALDs) and the homologues are present in bacteria and fungi, phylogenetic tree, distribution, and evolution of SALD, overview. Key residues in SALDs are analyzed by evolutionary methods and a molecular simulation analysis. The catalytic residue is most highly conserved, followed by the residues binding NAD+ and then the residues binding salicylaldehyde, molecular simulation analysis
Alteromonas naphthalenivorans
malfunction
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis. Cys284 is positioned close to both NAD+ and SAL, implicating it as a potentially important residue
Alteromonas naphthalenivorans
metabolism
the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway
Alteromonas naphthalenivorans
additional information
substrate binding induces a conformational change
Alteromonas naphthalenivorans
physiological function
salicylaldehyde dehydrogenase is responsible for the oxidation of salicylaldehyde to salicylate using NAD+ as a cofactor in the naphthalene degradation pathway
Alteromonas naphthalenivorans
General Information (protein specific)
General Information
Commentary
Organism
evolution
network and phylogenetic analyses indicated that salicylaldehyde dehydrogenases (SALDs) and the homologues are present in bacteria and fungi, phylogenetic tree, distribution, and evolution of SALD, overview. Key residues in SALDs are analyzed by evolutionary methods and a molecular simulation analysis. The catalytic residue is most highly conserved, followed by the residues binding NAD+ and then the residues binding salicylaldehyde, molecular simulation analysis
Alteromonas naphthalenivorans
malfunction
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis. Cys284 is positioned close to both NAD+ and SAL, implicating it as a potentially important residue
Alteromonas naphthalenivorans
metabolism
the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway
Alteromonas naphthalenivorans
additional information
substrate binding induces a conformational change
Alteromonas naphthalenivorans
physiological function
salicylaldehyde dehydrogenase is responsible for the oxidation of salicylaldehyde to salicylate using NAD+ as a cofactor in the naphthalene degradation pathway
Alteromonas naphthalenivorans
Expression (protein specific)
Organism
Commentary
Expression
Alteromonas naphthalenivorans
SALD from Alteromonas naphthalenivorans (SALDan) is specifically upregulated in response to naphthalene
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1492
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
3992
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
5444
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
5668
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
5932
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
10568
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
32526
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
33370
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1492
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
3992
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
5444
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
Alteromonas naphthalenivorans
5668
-
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
5932
-
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
10568
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
Alteromonas naphthalenivorans
32526
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
Alteromonas naphthalenivorans
33370
-
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
Alteromonas naphthalenivorans
Other publictions for EC 1.2.1.65
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)
743833
Jia
Evolutionary, computational, ...
Alteromonas naphthalenivorans
Sci. Rep.
7
43489
2017
-
-
1
-
4
-
1
9
-
-
1
1
-
4
-
-
1
1
-
-
-
-
2
2
-
1
-
8
1
1
-
1
4
-
-
-
-
1
1
-
4
-
-
1
4
9
-
-
1
1
-
-
-
1
-
-
-
-
2
2
-
1
-
8
1
1
-
-
1
5
5
1
8
8
741638
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172
806-819
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-
-
-
-
-
12
9
-
6
1
1
-
2
-
-
1
-
-
-
1
-
26
1
-
-
-
7
1
-
-
2
7
-
-
-
-
-
2
-
-
-
-
12
7
9
-
6
1
1
-
-
-
1
-
-
1
-
26
1
-
-
-
7
1
-
-
-
-
1
1
-
7
7
741793
Singh
Metabolic regulation and chro ...
Pseudomonas sp. C6
Arch. Microbiol.
195
521-535
2013
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
723872
Coitinho
Expression, purification and p ...
Pseudomonas putida, Pseudomonas putida G7
Acta Crystallogr. Sect. F
68
93-97
2012
-
-
1
1
-
-
-
-
-
-
1
-
-
11
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725888
Li
Physiological role of the nove ...
Pseudomonas putida, Pseudomonas putida ND6
Microbiol. Res.
166
643-653
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
696505
Nayak
Metabolism of acenaphthylene v ...
Stenotrophomonas sp. RMSK
Biodegradation
20
837-843
2009
-
1
-
-
-
-
-
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1
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2
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-
1
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-
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2
-
2
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1
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1
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1
-
1
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-
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1
-
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1
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-
2
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
691830
Zhao
-
A novel salicylaldehyde dehydr ...
Pseudomonas putida, Pseudomonas putida ND6
Chin. Sci. Bull.
52
1942-1948
2007
-
1
1
-
-
-
8
4
-
4
1
-
-
4
-
-
1
-
-
-
-
-
28
1
-
-
1
-
-
-
-
1
-
2
-
-
2
2
2
-
-
-
-
15
-
4
-
5
2
-
-
-
-
2
-
-
-
-
28
2
-
-
2
-
-
-
-
2
-
-
-
-
-
-
288315
Manohar
Degradation of naphthalene by ...
Pseudomonas sp., Pseudomonas sp. NGK1
Indian J. Exp. Biol.
33
353-356
1995
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
1
1
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2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
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-
2
-
-
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-
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288316
Eaton
Bacterial metabolism of naphth ...
Pseudomonas putida, Pseudomonas putida PpG1064
J. Bacteriol.
174
7542-7554
1992
-
-
1
-
-
-
-
-
-
-
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2
-
6
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288317
Connors
Metabolism of naphthalene by p ...
Pseudomonas sp.
J. Bacteriol.
141
1052-1054
1980
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-
1
-
-
-
-
-
-
-
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1
-
1
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288318
Austen
-
Regulation of the plasmid-spec ...
Pseudomonas putida, Pseudomonas putida PpG7
J. Gen. Microbiol.
117
521-528
1980
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-
-
-
-
-
-
-
-
-
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2
-
5
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288319
Barnsley
Role and regulation of the ort ...
Pseudomonas putida, Pseudomonas putida PpG7, Pseudomonas sp.
J. Bacteriol.
125
404-408
1976
-
-
-
-
-
-
-
-
-
-
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3
-
6
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
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-
-
2
-
-
-
-
-
-
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-
3
-
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-
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2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288320
Barnsley
The induction of the enzymes o ...
Pseudomonas putida, Pseudomonas putida PpG7, Pseudomonas sp.
J. Gen. Microbiol.
88
193-196
1975
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-
-
-
-
-
-
-
-
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3
-
6
-
-
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-
-
2
3
-
3
-
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-
-
-
-
-
-
2
-
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-
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-
-
2
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
2
3
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288321
Shamsuzzaman
The regulation of naphthalene ...
Pseudomonas putida
Biochem. Biophys. Res. Commun.
60
582-589
1974
-
-
-
-
-
-
1
1
-
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-
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
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-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
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-