BRENDA - Enzyme Database show
show all sequences of 1.6.5.10

Improving kinetic or thermodynamic stability of an azoreductase by directed evolution

Brissos, V.; Goncalves, N.; Melo, E.; Martins, L.; PLoS ONE 9, e87209 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression in Escherichia coli strains Tuner(DE3) and KRX
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
additional information
improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
Pseudomonas putida
Q192R
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 60 min) relative to parental mutant variant B1G6
Pseudomonas putida
Q192R/A46P/V159A
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 90 min) relative to parental mutant variant 16B7
Pseudomonas putida
Q192R/A46P/V159A/A48P
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 2A1
Pseudomonas putida
Q192R/A46P/V159A/C129S
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 23C10
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A31S/K74E/A88G/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 2F11
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A77T/F98L/N131D
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 3B9
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A88G/N131D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 1B6
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/K74E/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 2E4
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/N131D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 6F11
Pseudomonas putida
Q192R/A46P/V159A/C129S/A77T/N131D
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 14D4
Pseudomonas putida
Q192R/A46P/V159A/C129S/D7H/A178D
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 13G10
Pseudomonas putida
Q192R/A46P/V159A/C129S/E36D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 1C11
Pseudomonas putida
Q192R/A46P/V159A/C129S/I6V/T79R/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 32F5
Pseudomonas putida
Q192R/A46P/V159A/C129S/K74E/A88G
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 23C5
Pseudomonas putida
Q192R/A46P/V159A/C129S/L161M/L169P
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 27E4
Pseudomonas putida
Q192R/A46P/V159A/C129S/N14D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 6F10
Pseudomonas putida
Q192R/A46P/V159A/C129S/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 23E4
Pseudomonas putida
Q192R/A46P/V159A/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 19E4
Pseudomonas putida
Q192R/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 90 min) relative to parental mutant variant 12B8
Pseudomonas putida
Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 60 min) relative to parental mutant variant K7E3
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
wild-type and mutant kinetics and thermodynamics, overview
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida MET94
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
743650
Pseudomonas putida
?
-
-
-
-
additional information
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
743650
Pseudomonas putida MET94
?
-
-
-
-
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
i.e. Lawsone
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
i.e. Lawsone
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,4-benzoquinone
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,4-benzoquinone
-
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + a quinone
-
743650
Pseudomonas putida
NADP+ + a quinol
-
-
-
?
NADPH + H+ + a quinone
-
743650
Pseudomonas putida MET94
NADP+ + a quinol
-
-
-
?
NADPH + H+ + anthraquinone-2-sulfonic acid
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + catechol
i.e. 1,2-dihydroxybenzene
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
-
Pseudomonas putida
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression in Escherichia coli strains Tuner(DE3) and KRX
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
Pseudomonas putida
Q192R
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 60 min) relative to parental mutant variant B1G6
Pseudomonas putida
Q192R/A46P/V159A
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 90 min) relative to parental mutant variant 16B7
Pseudomonas putida
Q192R/A46P/V159A/A48P
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 2A1
Pseudomonas putida
Q192R/A46P/V159A/C129S
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 23C10
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A31S/K74E/A88G/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 2F11
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A77T/F98L/N131D
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 3B9
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/A88G/N131D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 1B6
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/K74E/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 2E4
Pseudomonas putida
Q192R/A46P/V159A/C129S/A178D/N131D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 85C, 150 min) relative to parental mutant variant 6F11
Pseudomonas putida
Q192R/A46P/V159A/C129S/A77T/N131D
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 14D4
Pseudomonas putida
Q192R/A46P/V159A/C129S/D7H/A178D
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 13G10
Pseudomonas putida
Q192R/A46P/V159A/C129S/E36D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 1C11
Pseudomonas putida
Q192R/A46P/V159A/C129S/I6V/T79R/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 32F5
Pseudomonas putida
Q192R/A46P/V159A/C129S/K74E/A88G
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 23C5
Pseudomonas putida
Q192R/A46P/V159A/C129S/L161M/L169P
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 27E4
Pseudomonas putida
Q192R/A46P/V159A/C129S/N14D/L143Q
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 6F10
Pseudomonas putida
Q192R/A46P/V159A/C129S/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 80C, 60 min) relative to parental mutant variant 23E4
Pseudomonas putida
Q192R/A46P/V159A/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 60C, 45 min) relative to parental mutant variant 19E4
Pseudomonas putida
Q192R/Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 90 min) relative to parental mutant variant 12B8
Pseudomonas putida
Y179H
site-directed mutagenesis, analysis of initial activity and thermostability (at 55C, 60 min) relative to parental mutant variant K7E3
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
wild-type and mutant kinetics and thermodynamics, overview
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
743650
Pseudomonas putida
?
-
-
-
-
additional information
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
743650
Pseudomonas putida MET94
?
-
-
-
-
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
i.e. Lawsone
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
i.e. Lawsone
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,4-benzoquinone
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 1,4-benzoquinone
-
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
743650
Pseudomonas putida MET94
NADP+ + ?
-
-
-
?
NADPH + H+ + a quinone
-
743650
Pseudomonas putida
NADP+ + a quinol
-
-
-
?
NADPH + H+ + a quinone
-
743650
Pseudomonas putida MET94
NADP+ + a quinol
-
-
-
?
NADPH + H+ + anthraquinone-2-sulfonic acid
-
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
NADPH + H+ + catechol
i.e. 1,2-dihydroxybenzene
743650
Pseudomonas putida
NADP+ + ?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
-
Pseudomonas putida
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas putida
General Information
General Information
Commentary
Organism
physiological function
Pseudomonas putida MET94 is a bacteria that degrades a wide range of structurally distinct azo dyes with high efficiency and the azoreductase PpAzoR plays a key role in this process
Pseudomonas putida
General Information (protein specific)
General Information
Commentary
Organism
physiological function
Pseudomonas putida MET94 is a bacteria that degrades a wide range of structurally distinct azo dyes with high efficiency and the azoreductase PpAzoR plays a key role in this process
Pseudomonas putida
Other publictions for EC 1.6.5.10
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)
743650
Brissos
Improving kinetic or thermody ...
Pseudomonas putida, Pseudomonas putida MET94
PLoS ONE
9
e87209
2014
-
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1
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21
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1
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7
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-
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12
1
1
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1
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1
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21
-
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1
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-
-
12
1
1
-
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-
1
-
-
-
-
1
1
-
-
-
724333
Hervas
ArsH from the cyanobacterium S ...
Synechocystis sp.
Biochemistry
51
1178-1187
2012
-
-
1
-
-
-
2
9
-
-
-
1
-
1
-
-
-
1
-
-
-
-
10
-
1
-
-
7
1
-
-
1
-
-
1
-
-
1
1
-
-
-
1
2
-
9
-
-
-
1
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-
-
-
-
-
-
-
10
-
1
-
-
7
1
-
-
-
-
4
4
-
-
-
714708
Crosas
Novel alkenal/one reductase ac ...
Saccharomyces cerevisiae
Chem. Biol. Interact.
191
32-37
2011
-
-
-
1
-
-
-
2
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-
-
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1
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3
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2
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1
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2
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-
3
-
-
-
-
2
-
-
-
-
1
1
1
1
2
2
701035
Zai
Oxidative stress in tardive dy ...
Homo sapiens
Prog. Neuropsychopharmacol. Biol. Psychiatry
34
50-56
2009
-
1
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1
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1
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1
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1
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688840
Hong
The NADPH quinone reductase Md ...
Helicobacter hepaticus, Helicobacter hepaticus ATCC 51449
Microb. Pathog.
44
169-174
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
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6
1
1
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1
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2
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2
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1
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6
1
1
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-
1
-
-
-
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-
-
-
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-
690177
Huang
Arsenic methylation capability ...
Homo sapiens
Urol. Int.
80
405-412
2008
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1
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-
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-
-
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1
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1
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1
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1
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-
-
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-
-
-
-
-
695605
Wagner
The natural compound ascorbige ...
Rattus norvegicus
Ann. Nutr. Metab.
53
122-128
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
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-
-
2
-
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1
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1
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1
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2
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1
-
-
-
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-
-
-
-
-
-
-
-
-
696015
Endo
Human carbonyl reductase 4 is ...
Homo sapiens
Biochem. Biophys. Res. Commun.
377
1326-1330
2008
-
-
1
-
-
-
4
9
1
-
2
-
-
1
-
-
-
-
-
4
-
-
10
1
1
-
-
7
1
-
-
1
3
-
-
-
-
1
1
-
-
-
-
4
3
9
1
-
2
-
-
-
-
-
-
4
-
-
10
1
1
-
-
7
1
-
-
-
-
-
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-
-
-
699129
Lambertucci
Palmitate increases superoxide ...
Rattus norvegicus
J. Cell. Physiol.
216
796-804
2008
1
-
-
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1
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2
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1
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2
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1
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1
1
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2
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1
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2
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1
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2
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1
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1
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1
1
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