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show all sequences of 1.1.1.B4

Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans

Zhou, S.; Zhang, S.C.; Lai, D.Y.; Zhang, S.L.; Chen, Z.M.; Biotechnol. Lett. 35, 359-365 (2013)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
ethyl benzoylformate is asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95% conversion and in an enantiomeric excess of 99.9%
Carboxydothermus hydrogenoformans
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Carboxydothermus hydrogenoformans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.3
-
ethyl 2-oxopropanoate
pH 6.5, 50°C
Carboxydothermus hydrogenoformans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30000, SDS-PAGE and calculated
Carboxydothermus hydrogenoformans
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Acetone
10% v/v, 30% residual activity
Carboxydothermus hydrogenoformans
DMSO
10% v/v, 50% residual activity
Carboxydothermus hydrogenoformans
Ethanol
10% v/v, 50% residual activity
Carboxydothermus hydrogenoformans
tetrahydrofuran
10% v/v, 25% residual activity
Carboxydothermus hydrogenoformans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Carboxydothermus hydrogenoformans
Q3ACV3
-
-
Carboxydothermus hydrogenoformans DSM 6008
Q3ACV3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylpentan-2-one + NADH + H+
46% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
4-methylpentan-2-ol + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
4-methylpentan-2-one + NADH + H+
46% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
4-methylpentan-2-ol + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
cycloheptanone + NADH + H+
69% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
cycloheptanol + NAD+
-
-
-
?
cycloheptanone + NADH + H+
69% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
cycloheptanol + NAD+
-
-
-
?
ethyl 2-oxo-3-phenylpropanoate + NADH + H+
48% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxy-3-phenylpropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxo-3-phenylpropanoate + NADH + H+
48% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
ethyl 2-hydroxy-3-phenylpropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxo-4-phenylbutanoate + NADH + H+
135% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxy-4-phenylbutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxopropanoate + NADH + H+
-
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxypropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 3-oxohexanoate + NADH + H+
105% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 3-hydroxyhexanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
129% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 4-chloro-3-hydroxybutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
129% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
ethyl 4-chloro-3-hydroxybutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl benzoylformate + NADH + H+
270% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl (R)-mandelate+ NAD+
95% conversion with 99.9% enantiomeric excess
-
-
?
ethyl oxo(phenyl)acetate + NADH + H+
270% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl hydroxy(phenyl)acetate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
additional information
enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters
721911
Carboxydothermus hydrogenoformans
?
-
-
-
-
additional information
enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters
721911
Carboxydothermus hydrogenoformans DSM 6008
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 30000, SDS-PAGE and calculated
Carboxydothermus hydrogenoformans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
-
Carboxydothermus hydrogenoformans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.97
-
ethyl 2-oxopropanoate
pH 6.5, 50°C
Carboxydothermus hydrogenoformans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Carboxydothermus hydrogenoformans
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
preferred over NADPH
Carboxydothermus hydrogenoformans
NADPH
about 10% of the activity with NADH
Carboxydothermus hydrogenoformans
Application (protein specific)
Application
Commentary
Organism
synthesis
ethyl benzoylformate is asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95% conversion and in an enantiomeric excess of 99.9%
Carboxydothermus hydrogenoformans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Carboxydothermus hydrogenoformans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
preferred over NADPH
Carboxydothermus hydrogenoformans
NADPH
about 10% of the activity with NADH
Carboxydothermus hydrogenoformans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.3
-
ethyl 2-oxopropanoate
pH 6.5, 50°C
Carboxydothermus hydrogenoformans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30000, SDS-PAGE and calculated
Carboxydothermus hydrogenoformans
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Acetone
10% v/v, 30% residual activity
Carboxydothermus hydrogenoformans
DMSO
10% v/v, 50% residual activity
Carboxydothermus hydrogenoformans
Ethanol
10% v/v, 50% residual activity
Carboxydothermus hydrogenoformans
tetrahydrofuran
10% v/v, 25% residual activity
Carboxydothermus hydrogenoformans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-methylpentan-2-one + NADH + H+
46% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
4-methylpentan-2-ol + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
4-methylpentan-2-one + NADH + H+
46% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
4-methylpentan-2-ol + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
cycloheptanone + NADH + H+
69% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
cycloheptanol + NAD+
-
-
-
?
cycloheptanone + NADH + H+
69% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
cycloheptanol + NAD+
-
-
-
?
ethyl 2-oxo-3-phenylpropanoate + NADH + H+
48% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxy-3-phenylpropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxo-3-phenylpropanoate + NADH + H+
48% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
ethyl 2-hydroxy-3-phenylpropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxo-4-phenylbutanoate + NADH + H+
135% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxy-4-phenylbutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 2-oxopropanoate + NADH + H+
-
721911
Carboxydothermus hydrogenoformans
ethyl 2-hydroxypropanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 3-oxohexanoate + NADH + H+
105% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 3-hydroxyhexanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
129% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl 4-chloro-3-hydroxybutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
129% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans DSM 6008
ethyl 4-chloro-3-hydroxybutanoate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
ethyl benzoylformate + NADH + H+
270% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl (R)-mandelate+ NAD+
95% conversion with 99.9% enantiomeric excess
-
-
?
ethyl oxo(phenyl)acetate + NADH + H+
270% of the activity with ethyl 2-oxopropanoate
721911
Carboxydothermus hydrogenoformans
ethyl hydroxy(phenyl)acetate + NAD+
chirality of the product not determined. The enzyme prouces ethyl (R)-mandelate from ethal benzoylformate
-
-
?
additional information
enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters
721911
Carboxydothermus hydrogenoformans
?
-
-
-
-
additional information
enzyme exhibits reductase activity towards a broad spectrum of substrates including aliphatic linear, branched, and cyclic ketones, aromatic ketones, alpha-ketoesters, and beta-ketoesters. Both alpha- and beta-ketoesters serve as better substrates than ketones, but the enzymes shows a preference for alpha-ketoesters
721911
Carboxydothermus hydrogenoformans DSM 6008
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 30000, SDS-PAGE and calculated
Carboxydothermus hydrogenoformans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
-
Carboxydothermus hydrogenoformans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.97
-
ethyl 2-oxopropanoate
pH 6.5, 50°C
Carboxydothermus hydrogenoformans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Carboxydothermus hydrogenoformans
Other publictions for EC 1.1.1.B4
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)
721911
Zhou
Biocatalytic characterization ...
Carboxydothermus hydrogenoformans, Carboxydothermus hydrogenoformans DSM 6008
Biotechnol. Lett.
35
359-365
2013
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723841
Protsko
Crystallization and preliminar ...
Thermoanaerobacter ethanolicus
Acta Crystallogr. Sect. F
66
831-833
2010
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1
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725726
Li
-
Deracemization of aryl seconda ...
Microbacterium oxydans, Microbacterium oxydans ECU2010
J. Mol. Catal. B
64
48-52
2010
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1
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4
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697267
Pal
Activity of yeast alcohol dehy ...
Saccharomyces carlsbergensis, Saccharomyces carlsbergensis Y379-50, Saccharomyces cerevisiae
Chem. Biol. Interact.
178
16-23
2009
-
-
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1
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3
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3
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3
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697839
Pennacchio
Role of Tryptophan 95 in subst ...
Sulfolobus solfataricus
Extremophiles
13
751-761
2009
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1
1
1
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4
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1
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1
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1
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711860
Machielsen
-
Cofactor engineering of Lactob ...
Lactobacillus brevis
Eng. Life Sci.
9
38-44
2009
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5
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4
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5
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2
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4
4
684583
Pennacchio
Purification and characterizat ...
Thermus thermophilus
Appl. Environ. Microbiol.
74
3949-3958
2008
1
1
1
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7
5
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5
4
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1
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7
1
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4
4
2
2
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3
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1
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3
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7
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5
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5
4
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7
1
2
1
4
4
2
2
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688747
Nie
A novel NADH-dependent carbony ...
Candida parapsilosis
Lett. Appl. Microbiol.
44
555-562
2007
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1
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9
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1
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1
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1
1
10
1
1
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1
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687864
Isobe
Thermostable NAD+-dependent (R ...
Burkholderia sp., Burkholderia sp. AIU 652
J. Biosci. Bioeng.
96
387-393
2003
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6
15
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2
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3
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1
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1
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24
1
1
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1
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3
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3
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1
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-
-
3
-
-
-
-
6
-
15
-
-
2
-
-
-
-
1
-
-
1
-
24
1
1
-
1
-
3
-
-
1
-
-
-
-
-
-
688571
Bradshaw
-
A Pseudomonas sp. alcohol dehy ...
Pseudomonas sp., Pseudomonas sp. PED
J. Org. Chem.
57
1526-1532
1992
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2
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2
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1
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1
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24
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2
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2
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1
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24
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2
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