BRENDA - Enzyme Database show
show all sequences of 1.1.1.18

Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification

van Straaten, K.E.; Zheng, H.; Palmer, D.R.; Sanders, D.A.; Biochem. J. 432, 237-247 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene iolG
Bacillus subtilis
Crystallization (Commentary)
Crystallization
Organism
purified wild-type BsIDH and K97V mutant in apo-, holo- and ternary complexes with inositol and inosose, mixing of 0.002 ml of protein solution containing 10mg/ml protein in 25 mM Tris pH 8.0, with 0.002 ml reservoir solution containing 0.1-0.2 M tri-sodium citrate, pH 5.4, and 1.6-2.9 M ammonium sulfate, for the holo-enzyme complexes with 0.1 M tri-sodium citrate pH 5.4, 2.6 M ammonium sulfate and either inositol or inosose at 4 mg/0.1 ml mother liquid, cryoprotection with 25% ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution
Bacillus subtilis
Engineering
Amino acid exchange
Commentary
Organism
K97V
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
?
-
-
-
myo-inositol + NAD+
Bacillus subtilis
the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
scyllo-inosose + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
gene iolG
-
Reaction
Reaction
Commentary
Organism
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Lys97, Asp172, and His176 are the catalytic triad involved in the catalytic mechanism, overview
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
711151
Bacillus subtilis
?
-
-
-
-
additional information
structure-function analysis, overview
711151
Bacillus subtilis
?
-
-
-
-
myo-inositol + NAD+
-
711151
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
myo-inositol + NAD+
the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
711151
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
BsIDH is a tetramer, with an arrangement consisting of 2 long continuous beta-sheets, formed from all 4 monomers, in which the central 2 strands are crossed over to form the core of the tetramer. Each subunit in the tetramer consists of two domains, an N-terminal Rossmann fold domain containing the cofactor-binding site, and a C-terminal domain containing the inositol-binding site, structure-function analysis, overview
Bacillus subtilis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene iolG
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus subtilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified wild-type BsIDH and K97V mutant in apo-, holo- and ternary complexes with inositol and inosose, mixing of 0.002 ml of protein solution containing 10mg/ml protein in 25 mM Tris pH 8.0, with 0.002 ml reservoir solution containing 0.1-0.2 M tri-sodium citrate, pH 5.4, and 1.6-2.9 M ammonium sulfate, for the holo-enzyme complexes with 0.1 M tri-sodium citrate pH 5.4, 2.6 M ammonium sulfate and either inositol or inosose at 4 mg/0.1 ml mother liquid, cryoprotection with 25% ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K97V
site-directed mutagenesis, inactive mutant
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
?
-
-
-
myo-inositol + NAD+
Bacillus subtilis
the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
scyllo-inosose + NADH + H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
711151
Bacillus subtilis
?
-
-
-
-
additional information
structure-function analysis, overview
711151
Bacillus subtilis
?
-
-
-
-
myo-inositol + NAD+
-
711151
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
myo-inositol + NAD+
the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
711151
Bacillus subtilis
scyllo-inosose + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
BsIDH is a tetramer, with an arrangement consisting of 2 long continuous beta-sheets, formed from all 4 monomers, in which the central 2 strands are crossed over to form the core of the tetramer. Each subunit in the tetramer consists of two domains, an N-terminal Rossmann fold domain containing the cofactor-binding site, and a C-terminal domain containing the inositol-binding site, structure-function analysis, overview
Bacillus subtilis
General Information
General Information
Commentary
Organism
metabolism
inositol dehydrogenase is responsible for the first step in myo-inositol degradation
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
inositol dehydrogenase is responsible for the first step in myo-inositol degradation
Bacillus subtilis
Other publictions for EC 1.1.1.18
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)
723126
Yoshida
Three inositol dehydrogenases ...
Geobacillus kaustophilus, Geobacillus kaustophilus PS8
Microbiology
158
1942-1952
2012
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4
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1
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1
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1
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711151
van Straaten
Structural investigation of my ...
Bacillus subtilis
Biochem. J.
432
237-247
2010
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1
1
1
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4
1
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1
1
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712965
Morinaga
Identification of two scyllo-i ...
Bacillus subtilis 168, Bacillus subtilis
Microbiology
156
1538-1546
2010
-
-
1
-
1
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6
-
72
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10
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2
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1
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1
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6
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10
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1
1
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684205
Van Straaten
Purification, crystallization ...
Bacillus subtilis
Acta Crystallogr. Sect. F
64
98-101
2008
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-
1
1
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1
1
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1
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1
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1
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684557
Yebra
Identification of a gene clust ...
Lactobacillus casei
Appl. Environ. Microbiol.
73
3850-3858
2007
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1
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1
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685170
Daniellou
Probing the promiscuous active ...
Bacillus subtilis
Biochemistry
46
7469-7477
2007
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6
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1
12
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1
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2
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1
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15
1
1
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6
1
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2
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2
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6
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1
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12
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1
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15
1
1
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6
1
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668169
Daniellou
Appel-Lee synthesis of glycosy ...
Bacillus subtilis
Carbohydr. Res.
341
2145-2150
2006
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1
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1
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670456
Daniellou
Stereoselective oxidation of p ...
Bacillus subtilis
Org. Biomol. Chem.
3
401-403
2005
-
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-
-
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7
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2
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8
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1
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1
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7
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8
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655247
Yamakoshi
Determination of urinary myo-i ...
Flavobacterium sp.
Clin. Chim. Acta
328
163-171
2003
-
1
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-
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1
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3
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3
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1
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1
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1
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1
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656606
Ono
Specific determination of myo- ...
Enterobacter aerogenes
J. Pharm. Biomed. Anal.
33
1175-1180
2003
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1
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1
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389427
Jiang
A functional myo-inositol dehy ...
Sinorhizobium fredii, Sinorhizobium fredii USDA191
J. Bacteriol.
183
2595-2604
2001
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-
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1
2
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2
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1
1
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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
1
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1
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389428
Galbraith
A functional myo-inositol cata ...
Sinorhizobium meliloti
Microbiology
144
2915-2924
1998
-
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1
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389429
Stein
myo-Inositol dehydrogenase fro ...
Galdieria sulphuraria
Phytochemistry
46
17-20
1997
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2
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3
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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389430
Fujita
Bacillus subtiltis inositol de ...
Bacillus subtilis
Gene
108
121-125
1991
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389431
Ramaley
Purification and properties of ...
Bacillus subtilis
J. Biol. Chem.
254
7684-7690
1979
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5
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5
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1
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4
1
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389432
Fawole
Inositol dehydrogenase from Se ...
Serratia marcescens
Z. Allg. Mikrobiol.
16
327-328
1976
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389435
Alizade
Chirality of the hydrogen tran ...
Klebsiella pneumoniae
Z. Naturforsch. C
31
624-625
1976
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3
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389433
Walker
myo-Inositol:NAD+ 2-oxidoreduc ...
Streptomyces hygroscopicus
Methods Enzymol.
43
433-439
1975
-
-
-
-
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2
-
1
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1
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2
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2
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2
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2
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1
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2
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389434
Criddle
myo-Inositol dehydrogenase(s) ...
Gluconobacter oxydans
Biochem. J.
137
449-452
1974
-
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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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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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1
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389436
Vidal-Leiria
Inositol dehydrogenase from th ...
Myxozyma melibiosi
Biochim. Biophys. Acta
293
295-303
1973
-
-
-
-
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2
-
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5706
Berman
The pathway of myo-inositol de ...
Enterobacter aerogenes
J. Biol. Chem.
241
800-806
1966
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