BRENDA - Enzyme Database show
show all sequences of 3.6.1.28

Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase

Delvaux, D.; Kerff, F.; Murty, M.R.; Lakaye, B.; Czerniecki, J.; Kohn, G.; Wins, P.; Herman, R.; Gabelica, V.; Heuze, F.; Tordoir, X.; Maree, R.; Matagne, A.; Charlier, P.; De Pauw, E.; Bettendorff, L.; Biochim. Biophys. Acta 1830, 4513-4523 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Homo sapiens
-
Mus musculus
Crystallization (Commentary)
Crystallization
Organism
complex with tripolyphosphate, to 2.3 A resolution and docking solution of substrate thiamine triphosphate. The thiazole ring of the thiamine forms a stacking interaction with Trp53, and the aminopyrimidine ring lies in a pocket defined by His76, Pro191 and Ile195. The triphosphate moiety occupies a similar position as in the enzyme-tripolyphosphate complex, with interactions involving the side chains of Lys11, Arg55, Arg57, Lys65, Arg125 and Lys193
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
D147A
about 30% of wild-type catalytic efficiency
Mus musculus
D37A
about 0.5% of wild-type catalytic efficiency
Mus musculus
E81A
about 30% of wild-type catalytic efficiency
Mus musculus
K11A
about 15% of wild-type catalytic efficiency
Mus musculus
K193A
about 60% of wild-type catalytic efficiency
Mus musculus
K65A
more than 1000fold decrease in kcat value
Mus musculus
W53A
2.5fold increase in catalytic efficiency
Mus musculus
Y39A
about 30% of wild-type catalytic efficiency
Mus musculus
Y79A
about 5% of wild-type catalytic efficiency
Mus musculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.008
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
0.009
-
thiamine triphosphate
mutant K65A, pH 8.5, 37°C
Mus musculus
0.012
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C
Mus musculus
0.013
-
thiamine triphosphate
mutant E81A, pH 8.5, 37°C
Mus musculus
0.042
-
thiamine triphosphate
mutant Y79A, pH 8.5, 37°C
Mus musculus
0.2
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
0.55
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
0.62
-
thiamine triphosphate
mutant Y39A, pH 8.5, 37°C
Mus musculus
0.74
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C
Mus musculus
2.8
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C
Mus musculus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for catalytic activity, not required for substrate binding
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q9BU02
-
-
Mus musculus
Q8JZL3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thiamine triphosphate + H2O
-
733393
Mus musculus
thiamine diphosphate + phosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.019
-
thiamine triphosphate
mutant K65A, pH 8.5, 37°C
Mus musculus
0.64
-
thiamine triphosphate
mutant Y39A, pH 8.5, 37°C
Mus musculus
1.5
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C
Mus musculus
2.6
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C
Mus musculus
2.8
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
4.4
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
6
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C; mutant Y79A, pH 8.5, 37°C
Mus musculus
14.1
-
thiamine triphosphate
mutant E81A, pH 8.5, 37°C
Mus musculus
23
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
-
Mus musculus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
complex with tripolyphosphate, to 2.3 A resolution and docking solution of substrate thiamine triphosphate. The thiazole ring of the thiamine forms a stacking interaction with Trp53, and the aminopyrimidine ring lies in a pocket defined by His76, Pro191 and Ile195. The triphosphate moiety occupies a similar position as in the enzyme-tripolyphosphate complex, with interactions involving the side chains of Lys11, Arg55, Arg57, Lys65, Arg125 and Lys193
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D147A
about 30% of wild-type catalytic efficiency
Mus musculus
D37A
about 0.5% of wild-type catalytic efficiency
Mus musculus
E81A
about 30% of wild-type catalytic efficiency
Mus musculus
K11A
about 15% of wild-type catalytic efficiency
Mus musculus
K193A
about 60% of wild-type catalytic efficiency
Mus musculus
K65A
more than 1000fold decrease in kcat value
Mus musculus
W53A
2.5fold increase in catalytic efficiency
Mus musculus
Y39A
about 30% of wild-type catalytic efficiency
Mus musculus
Y79A
about 5% of wild-type catalytic efficiency
Mus musculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.008
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
0.009
-
thiamine triphosphate
mutant K65A, pH 8.5, 37°C
Mus musculus
0.012
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C
Mus musculus
0.013
-
thiamine triphosphate
mutant E81A, pH 8.5, 37°C
Mus musculus
0.042
-
thiamine triphosphate
mutant Y79A, pH 8.5, 37°C
Mus musculus
0.2
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
0.55
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
0.62
-
thiamine triphosphate
mutant Y39A, pH 8.5, 37°C
Mus musculus
0.74
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C
Mus musculus
2.8
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C
Mus musculus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for catalytic activity, not required for substrate binding
Mus musculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thiamine triphosphate + H2O
-
733393
Mus musculus
thiamine diphosphate + phosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.019
-
thiamine triphosphate
mutant K65A, pH 8.5, 37°C
Mus musculus
0.64
-
thiamine triphosphate
mutant Y39A, pH 8.5, 37°C
Mus musculus
1.5
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C
Mus musculus
2.6
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C
Mus musculus
2.8
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
4.4
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
6
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C; mutant Y79A, pH 8.5, 37°C
Mus musculus
14.1
-
thiamine triphosphate
mutant E81A, pH 8.5, 37°C
Mus musculus
23
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
14
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
140
-
thiamine triphosphate
mutant Y79A, pH 8.5, 37°C
Mus musculus
500
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C
Mus musculus
1000
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C; mutant E81A, pH 8.5, 37°C; mutant Y39A, pH 8.5, 37°C
Mus musculus
2000
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C; mutant K65A, pH 8.5, 37°C
Mus musculus
3000
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
8000
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
14
-
thiamine triphosphate
mutant D37A, pH 8.5, 37°C
Mus musculus
140
-
thiamine triphosphate
mutant Y79A, pH 8.5, 37°C
Mus musculus
500
-
thiamine triphosphate
mutant K11A, pH 8.5, 37°C
Mus musculus
1000
-
thiamine triphosphate
mutant D147A, pH 8.5, 37°C; mutant E81A, pH 8.5, 37°C; mutant Y39A, pH 8.5, 37°C
Mus musculus
2000
-
thiamine triphosphate
mutant K193A, pH 8.5, 37°C; mutant K65A, pH 8.5, 37°C
Mus musculus
3000
-
thiamine triphosphate
wild-type, pH 8.5, 37°C
Mus musculus
8000
-
thiamine triphosphate
mutant W53A, pH 8.5, 37°C
Mus musculus
Other publictions for EC 3.6.1.28
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)
733393
Delvaux
Structural determinants of spe ...
Homo sapiens, Mus musculus
Biochim. Biophys. Acta
1830
4513-4523
2013
-
-
2
1
9
-
-
10
-
1
-
-
-
2
-
-
-
-
-
-
-
-
1
-
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9
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2
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1
9
-
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10
-
1
-
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-
-
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-
1
-
-
-
-
9
-
-
-
-
-
-
-
-
7
7
687693
Song
Structural basis for the catal ...
Mus musculus
J. Biol. Chem.
283
10939-10948
2008
-
-
-
-
-
-
1
1
1
1
1
1
-
2
-
-
-
1
-
-
-
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2
1
1
-
-
-
1
-
-
-
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-
-
-
1
-
1
1
1
1
1
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
696404
Kovacevic
The iron-regulated metastasis ...
Homo sapiens, Rattus norvegicus
Biochim. Biophys. Acta
1783
1981-1992
2008
2
-
2
-
2
-
-
-
-
-
-
2
-
2
-
-
-
-
-
3
-
-
4
-
-
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-
-
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-
-
-
-
2
-
2
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2
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2
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3
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4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667797
Szyniarowski Piot
Pig tissues express a catalyti ...
Homo sapiens, Sus scrofa
Biochim. Biophys. Acta
1725
93-102
2005
-
-
2
-
4
-
2
3
-
5
2
-
-
6
-
-
2
-
-
1
16
-
2
-
-
-
1
-
5
-
-
-
2
-
1
-
-
2
-
-
4
-
1
2
2
3
-
5
2
-
-
-
-
2
-
1
16
-
2
-
-
-
1
-
5
-
-
-
-
-
-
-
-
-
655738
Lakaye
Human recombinant thiamine tri ...
Homo sapiens
Int. J. Biochem. Cell Biol.
36
1348-1364
2004
-
-
1
-
-
-
6
2
1
2
-
-
-
3
-
-
1
-
-
-
1
-
2
-
-
-
2
2
1
1
-
-
2
-
1
-
-
1
-
-
-
-
1
7
2
2
1
2
-
-
-
-
-
1
-
-
1
-
2
-
-
-
2
2
1
1
-
-
-
-
-
-
-
-
656873
Czerniecki
Neuronal localization of the 2 ...
Rattus norvegicus
Neuroscience
125
833-840
2004
-
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668963
Lakaye
Expression of 25 kDa thiamine ...
Mus musculus, Rattus norvegicus
Int. J. Biochem. Cell Biol.
36
2032-2041
2004
-
-
-
-
-
-
-
1
-
-
-
-
-
5
-
-
-
-
-
16
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
16
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655198
Makarchikov
Thiamine triphosphate and thia ...
Bos taurus, Gallus gallus, Homo sapiens, quail, Rattus norvegicus, Sus scrofa
Cell. Mol. Life Sci.
60
1477-1488
2003
-
-
-
-
-
-
-
15
-
-
17
-
-
12
-
-
-
-
-
25
22
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
15
-
-
17
-
-
-
-
-
-
25
22
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656042
Lakaye
Molecular characterization of ...
Bos taurus, Homo sapiens
J. Biol. Chem.
277
13771-13777
2002
-
-
1
-
-
-
4
2
1
-
6
-
-
7
-
-
2
-
-
9
2
-
4
2
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
2
1
-
6
-
-
-
-
2
-
9
2
-
4
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
210023
Makarchikov
Thiamine triphosphatase activi ...
Bos taurus
Biochem. Mol. Biol. Int.
46
115-123
1998
-
-
-
-
-
-
-
2
-
-
1
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
210021
Bettendorff
Thiamine, thiamine phosphates, ...
Homo sapiens
J. Neurochem.
66
250-258
1996
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
210020
Makarchikov
Purification and characterizat ...
Bos taurus
Biochim. Biophys. Acta
1117
326-332
1992
-
-
-
-
-
1
-
1
1
6
2
-
-
2
-
-
1
-
-
2
1
2
7
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
1
6
2
-
-
-
-
1
-
2
1
2
7
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
210012
Matsuda
Membrane-associated thiamine t ...
Rattus norvegicus
Int. J. Biochem.
23
1111-1114
1991
-
-
-
-
-
-
9
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
1
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
210022
Bettendorff
Solubilization and thiamine tr ...
Electrophorus electricus
Biochim. Biophys. Acta
1073
69-76
1991
4
-
-
-
-
-
3
-
1
-
-
-
-
2
-
-
-
-
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
210024
Bettendorff
Application of high-performanc ...
Electrophorus electricus
J. Chromatogr.
566
397-408
1991
-
-
-
-
-
-
-
-
-
1
-
1
-
3
-
-
-
-
-
1
-
-
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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-
210019
Nishimune
Hydrolysis and synthesis of th ...
Aneurinibacillus aneurinilyticus, Escherichia coli, Escherichia coli W 1485
J. Nutr. Sci. Vitaminol.
33
113-127
1987
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3
2
2
1
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3
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2
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2
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1
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3
1
2
2
1
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-
3
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2
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2
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210018
Ogawa
Recent findings on ultracytoch ...
Rattus norvegicus
Ann. N. Y. Acad. Sci.
378
188-214
1982
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-
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4
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1
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1
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4
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3
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2
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210017
Penttinen
The relation of the soluble th ...
Rattus norvegicus
Med. Biol.
59
177-184
1981
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-
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2
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2
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7
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2
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7
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210013
Barchi
Membrane-associated thiamin tr ...
Rattus norvegicus
J. Biol. Chem.
251
193-197
1976
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1
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1
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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1
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1
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1
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210014
Barchi
Membrane thiamine triphosphata ...
Rattus norvegicus
J. Neurochem.
26
715-720
1976
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4
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1
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2
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2
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1
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4
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1
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2
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1
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210011
Iwata
Properties of thiamine di- and ...
Rattus norvegicus
J. Neurochem.
24
1209-1213
1975
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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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4
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2
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1
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1
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210009
Iwata
Role of thiamine metabolism in ...
Rattus norvegicus
Jpn. J. Pharmacol.
24
825-829
1974
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2
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1
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2
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3
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1
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1
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3
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1
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210010
Iwata
Role of thiamine metabolism in ...
Rattus norvegicus
Jpn. J. Pharmacol.
24
817-823
1974
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1
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3
2
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2
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3
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4
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3
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1
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3
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4
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3
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210015
Iwata
-
Some properties of the enzyme ...
Rattus norvegicus
Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)
2. Meeting
213-221
1974
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4
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2
2
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1
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2
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1
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4
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2
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2
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1
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210016
Barchi
-
Thiamine triphosphatases in br ...
Rattus norvegicus
Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)
195-212
1974
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5
2
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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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1
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2
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5
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2
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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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2
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210006
Barchi
A membrane-associated thiamine ...
Rattus norvegicus
J. Biol. Chem.
247
7668-7673
1972
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3
3
1
8
1
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2
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1
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8
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1
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1
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2
2
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3
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3
1
8
1
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1
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8
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1
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1
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2
2
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210007
Hashitani
The partial purification of th ...
Rattus norvegicus
J. Biol. Chem.
247
2117-2119
1972
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4
1
1
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2
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6
1
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4
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4
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1
1
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6
1
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4
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210008
Barchi
Thiamine triphosphatase in the ...
Rattus norvegicus
Biochim. Biophys. Acta
255
402-405
1972
1
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1
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