BRENDA - Enzyme Database
show all sequences of 1.1.1.282

Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum

Kubota, T.; Tanaka, Y.; Hiraga, K.; Inui, M.; Yukawa, H.; Appl. Microbiol. Biotechnol. 97, 8139-8149 (2013)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene qsuD, recombinant expression in Escherichia coli
Corynebacterium glutamicum
Engineering
Protein Variants
Commentary
Organism
additional information
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
Corynebacterium glutamicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis constant with quinate as substrate is lower than that with shikimate under optimal conditions
Corynebacterium glutamicum
0.42
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
0.444
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
1.141
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
1.299
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
5.933
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
-
Corynebacterium glutamicum
60000
-
about, gel filtration
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-quinate + NAD+
Corynebacterium glutamicum
-
3-dehydroquinate + NADH + H+
-
-
?
shikimate + NAD+
Corynebacterium glutamicum
-
3-dehydroshikimate + NADH + H+
-
-
?
shikimate + NAD+
Corynebacterium glutamicum JCM 18229
-
3-dehydroshikimate + NADH + H+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Corynebacterium glutamicum
A4QB65
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme from Escherichia coli
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-quinate + NAD+
-
724089
Corynebacterium glutamicum
3-dehydroquinate + NADH + H+
-
-
-
?
additional information
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
724089
Corynebacterium glutamicum
?
-
-
-
?
additional information
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
724089
Corynebacterium glutamicum JCM 18229
?
-
-
-
?
shikimate + NAD+
-
724089
Corynebacterium glutamicum
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
-
724089
Corynebacterium glutamicum JCM 18229
3-dehydroshikimate + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 30000, about, recombinant enzyme, SDS-PAGE
Corynebacterium glutamicum
Synonyms
Synonyms
Commentary
Organism
cgR_0495
-
Corynebacterium glutamicum
qsuD
-
Corynebacterium glutamicum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.75
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
5.67
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
9.31
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
14.6
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
114
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction of 3-dehydroquinate with NADH
Corynebacterium glutamicum
8.5
-
oxidation of quinate with NAD+
Corynebacterium glutamicum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
the catalytic reaction of QsuD is highly susceptible to pH
Corynebacterium glutamicum
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme
Corynebacterium glutamicum
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene qsuD, recombinant expression in Escherichia coli
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme
Corynebacterium glutamicum
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown
Corynebacterium glutamicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis constant with quinate as substrate is lower than that with shikimate under optimal conditions
Corynebacterium glutamicum
0.42
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
0.444
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
1.141
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
1.299
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
5.933
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
-
Corynebacterium glutamicum
60000
-
about, gel filtration
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-quinate + NAD+
Corynebacterium glutamicum
-
3-dehydroquinate + NADH + H+
-
-
?
shikimate + NAD+
Corynebacterium glutamicum
-
3-dehydroshikimate + NADH + H+
-
-
?
shikimate + NAD+
Corynebacterium glutamicum JCM 18229
-
3-dehydroshikimate + NADH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-quinate + NAD+
-
724089
Corynebacterium glutamicum
3-dehydroquinate + NADH + H+
-
-
-
?
additional information
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
724089
Corynebacterium glutamicum
?
-
-
-
?
additional information
QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor
724089
Corynebacterium glutamicum JCM 18229
?
-
-
-
?
shikimate + NAD+
-
724089
Corynebacterium glutamicum
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
-
724089
Corynebacterium glutamicum JCM 18229
3-dehydroshikimate + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 30000, about, recombinant enzyme, SDS-PAGE
Corynebacterium glutamicum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.75
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
5.67
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
9.31
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
14.6
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
114
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction of 3-dehydroquinate with NADH
Corynebacterium glutamicum
8.5
-
oxidation of quinate with NAD+
Corynebacterium glutamicum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
the catalytic reaction of QsuD is highly susceptible to pH
Corynebacterium glutamicum
Expression
Organism
Commentary
Expression
Corynebacterium glutamicum
qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells
up
General Information
General Information
Commentary
Organism
physiological function
QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
Corynebacterium glutamicum
General Information (protein specific)
General Information
Commentary
Organism
physiological function
QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
Corynebacterium glutamicum
Expression (protein specific)
Organism
Commentary
Expression
Corynebacterium glutamicum
qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.96
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
1.35
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
8.16
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
32.88
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
271.4
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.96
-
3-dehydroshikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
1.35
-
shikimate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
8.16
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH
Corynebacterium glutamicum
32.88
-
L-quinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+
Corynebacterium glutamicum
271.4
-
3-dehydroquinate
pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH
Corynebacterium glutamicum
Other publictions for EC 1.1.1.282
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
Synonyms
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)
740881
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6
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-
2
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-
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1
1
2
-
1
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-
-
-
-
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6
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5
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4
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9
2
2
2
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4
2
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-
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-
-
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2
2
4
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1
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2
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1
2
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5
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3
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1
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7
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3
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1
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-
4
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Kubota
Characterization of shikimate ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
-
-
1
-
1
-
-
6
-
-
2
3
-
1
-
-
1
-
-
-
-
-
5
1
3
-
-
-
5
2
1
-
3
-
-
-
-
-
1
3
-
1
-
-
-
-
6
-
-
2
3
-
-
-
1
-
-
-
-
5
1
-
-
-
5
2
1
-
-
1
1
1
1
5
5
727115
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7
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-
-
-
-
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5
1
4
1
-
-
8
2
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3
-
-
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-
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3
1
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8
-
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5
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-
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-
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-
-
6
1
2
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-
-
6
-
-
-
3
-
-
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-
-
1
3
1
4
-
-
-
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6
-
1
-
4
-
-
-
1
-
-
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6
1
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6
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-
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1
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6
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3
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-
-
-
3
11
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6
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-
-
4
-
-
-
3
-
-
-
-
-
3
3
-
-
-
-
-
-
4
-
-
-
-
-
-
-
3
-
-
-
3
11
-
-
-
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4
-
-
-
-
-
-
-
-
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-
667700
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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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280
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-
-
30
-
-
3
-
-
3
-
-
-
-
-
-
-
-
4
1
2
-
-
-
30
-
-
-
4
-
-
-
-
2
-
4
-
8
-
-
-
-
30
-
-
3
-
-
-
-
-
-
-
-
-
4
1
-
-
-
30
-
-
-
-
-
-
-
-
-
-
669328
Singh
Crystal structure of a novel s ...
Enterococcus faecalis, Enterococcus faecium, Lactiplantibacillus plantarum, Listeria monocytogenes, Salmonella enterica subsp. enterica serovar Typhimurium, Shigella flexneri, Streptococcus pyogenes, Escherichia coli, Haemophilus influenzae
J. Biol. Chem.
280
17101-17108
2005
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-
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9
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9
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18
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8
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8
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9
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644536
Michel
Structures of shikimate dehydr ...
Escherichia coli
J. Biol. Chem.
278
19463-19472
2003
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-
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1
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8
-
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1
1
-
4
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1
2
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1
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4
1
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1
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6
1
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2
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2
1
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8
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1
1
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1
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1
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4
1
1
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6
1
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644537
Benach
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