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Information on EC 3.6.1.28 - thiamine-triphosphatase
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3.6.1.28 thiamine-triphosphataseSpecify your search results
Word Map
- 3.6.1.28
-
adenylyl
- electricus
- electrophorus
-
phosphohydrolases
- hydrophila
- tdp
- nitrosomonas
- diphosphatase
-
triphosphorylated
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
thiamine triphosphatase, thtpase, ttpase, thtpa, 25-kda thiamine triphosphatase, 25 kda thiamine triphosphatase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
25 kDa thiamine triphosphatase
25-kDa thiamine triphosphatase
phosphatase, thiamine tri-
-
-
-
-
thiamine triphosphatase
Thtpa
ThTPase
TTPase
-
-
-
-
thiamine triphosphatase
-
-
-
-
ThTPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thiamine triphosphate + H2O = thiamine diphosphate + phosphate
-
-
-
-
thiamine triphosphate + H2O = thiamine diphosphate + phosphate
catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoric ester hydrolysis
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thiamine-triphosphate phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9068-47-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
the catalytic efficiency is about 4 orders of magnitude lower than for thiamine triphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
no activity with enzyme from brain and liver
-
-
?
ATP + H2O
ADP + phosphate
-
4% of the activity with thiamine triphosphate
-
-
?
CTP + H2O
CDP + phosphate
-
at 13% of the activity with thiamine triphosphate
-
-
?
CTP + H2O
CDP + phosphate
-
18% of the activity with thiamine triphosphate with liver enzyme, no activity with brain enzyme
-
-
?
GTP + H2O
GDP + phosphate
-
at 13% of the activity with thiamine triphosphate
-
-
?
GTP + H2O
GDP + phosphate
-
14% of the activity with thiamine triphosphate with liver enzyme, no activity with brain enzyme
-
-
?
GTP + H2O
GDP + phosphate
-
at 4% of the activity with thiamine triphosphate
-
-
?
ITP + H2O
IDP + phosphate
-
18% of the activity with thiamine triphosphate with liver enzyme, no activity with brain enzyme
-
-
?
thiamine diphosphate + H2O
thiamine monophosphate + phosphate
-
28% of the activity with thiamine triphosphate with liver enzyme, 6% of the activity with thiamine triphosphate with brain enzyme
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
absolute specificity
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
thiamine triphosphate may play an important role in the regulation of Cl- permeability
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
absolute specificity
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
the enzyme is very specific for thiamine triphosphate, mechanism, overview, binding of Mg2+ induces only a minor local conformational change, whereas ThTP binding causes a more global conformational change, free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold, overview
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
210008, 210009, 210010, 210011, 210012, 210013, 210014, 210015, 210016, 210017, 210018, 656873, 668963
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
enzyme is involved in thiamine metabolism
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
the enzyme may play a general role in neuronal metabolism rather than a specific role in excitability. There is no apparent correlation between enzyme expression and selective vulnerability of certain brain regions to thiamine deficiency
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
thiamine triphosphate as Mg2+-thiamine triphosphate complex
-
-
?
UTP + H2O
UDP + phosphate
-
29% of the activitry with thiamine triphosphate with liver enzyme, no activity with brain enzyme
-
-
?
UTP + H2O
UDP + phosphate
-
at 2% of the activity with thiamine triphosphate
-
-
?
additional information
?
-
-
Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
-
-
?
additional information
?
-
Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
thiamine triphosphate may play an important role in the regulation of Cl- permeability
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
-
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
enzyme is involved in thiamine metabolism
-
?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
-
the enzyme may play a general role in neuronal metabolism rather than a specific role in excitability. There is no apparent correlation between enzyme expression and selective vulnerability of certain brain regions to thiamine deficiency
-
-
?
additional information
?
-
-
Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
-
-
?
additional information
?
-
Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Br-
-
stimulation by anions with the following order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme
Ca2+
Cl-
-
stimulation by anions with the following decreasing order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme
I-
-
stimulation by anions with the following decreasing order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme
Mg2+
Mn2+
NO3-
-
stimulation by anions with the following decreasing order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme. The effect of NO3- is maximal at pH 7-8, it is negligible at pH 6.5
SCN-
-
stimulation by anions with the following decreasing order of effectiveness: SCN-, I-, NO3-, Br-, Cl-, membrane-associated enzyme
Zn2+
Ca2+
-
the addition of Ca2+ at 5 mM concentration enhances the rate of thiamine triphosphate hydrolysis by a factor of 17-20
Ca2+
-
divalent cation requirement is fullfilled by Mg2+ or Ca2+ in microsomes and by Mg2+ but not Ca2+ in soluble fraction
Ca2+
-
divalent cation requirement is satisfied by Mg2+, Mn2+ or Ca2+
Mg2+
-
soluble enzyme requires Mg2+, enzyme from membrane is Mg2+-independent
Mg2+
-
the addition of Mg2+ at 5 mM concentration enhances the rate of thiamine triphosphate hydrolysis by a factor of 17-20
Mg2+
the enzyme has an absolute requirement for divalent cations, binding of Mg2+ induces only a minor local conformational change
Mg2+
-
divalent cation requirement is fullfilled by Mg2+ or Ca2+ in microsomes and by Mg2+ but not Ca2+ in soluble fraction
Mg2+
-
maximal activation occurs at a cation to substrate ratio of 1:1
Mg2+
-
divalent cation requirement is satisfied by Mg2+, Mn2+ or Ca2+
Mn2+
-
divalent cation requirement is satisfied by Mg2+, Mn2+ or Ca2+
Zn2+
-
0.01-0.05 mM at pH 8.0 activates GST-tagged thiamine triphosphatase by about 30% in the presence of Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
([2-[3-(4-Amino-2-methyl-pyrimidin-5-ylmethyl)-4-methyl-thiazol-5-yl]-ethoxy]-phosphonomethyl-phosphinoylmethyl)-phosphonic acid
-
-
1-[(4-amino-2-methyl-5-pyrimidinyl)methyl]-3-(2-hydroxyethyl)-2-methylpyridinium
-
soluble enzyme: 50% inhibition at 2 mM. Membrane-bound enzyme: no inhibition up to 5 mM
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid
-
1.0 mM, 62% inhibition of membrane-associated enzyme
4-acetamide-4'-isothiocyanostilbene-2,2'-disulfonic acid
-
1.0 mM, 36% inhibition of membrane-associated enzyme
SDS
-
IC50: about 0.3% W/v. The inhibition is partially reversible, probably due to correct refolding of the denatured enzyme
ADP
-
1 mM, strongly inhibits membrane-associated enzyme, soluble enzyme is unaffected
ATP
-
soluble enzyme: no inhibition up to 2 mM, membrane-bound enzyme: 50% inhibition at 5 mM
ATP
-
1 mM, strongly inhibits membrane-associated enzyme, soluble enzyme is unaffected
Ca2+
-
soluble enzyme: 50% inhibition at 5 mM, membrane-bound enzyme: 20% inhibition at 5 mM
chlorpromazine
-
microsomal and soluble enzyme; no inhibition in presence of Ca2+
NO3-
-
inhibition at pH 6.0. At pH 7.6 slight but consistent activation at 50 mM NO3-, higher concentrations are inhibitory
thiamine diphosphate
-
soluble enzyme, at levels of substrate 2 to 3 times Km, no inhibition of membrane-associated enzyme
Zn2+
-
inhibits at micromolar concentrations at pH 8.0, IC50: about 0.015-0.02 mM. Activates at pH 6.0
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
-
additional information
overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
High-throughput proteomics of breast cancer interstitial fluid: identification of tumor subtype-specific serologically relevant biomarkers.
Thiamine Deficiency
Neuronal localization of the 25-kDa specific thiamine triphosphatase in rodent brain.
Thiamine Deficiency
Role of thiamine metabolism in the central nervous system. II. Effects of various agents on thiamine triphosphatase activity in rat brain.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
thiamine triphosphate
-
membrane-associated enzyme, activated by Ca2+ or Mg2+
1.7 - 2.2
thiamine triphosphate
-
apparent value, in the presence of 5 mM Mg2+, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
([2-[3-(4-Amino-2-methyl-pyrimidin-5-ylmethyl)-4-methyl-thiazol-5-yl]-ethoxy]-phosphonomethyl-phosphinoylmethyl)-phosphonic acid
-
-
2
1-[(4-amino-2-methyl-5-pyrimidinyl)methyl]-3-(2-hydroxyethyl)-2-methylpyridinium
-
soluble enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015 - 0.02
Zn2+
Homo sapiens
-
inhibits at micromolar concentrations at pH 8.0, IC50: about 0.015-0.02 mM. Activates at pH 6.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
0.041
-
purified GST-tagged thiamine triphosphatase, 37°C, pH 8.2, 4 mM MgCl2, 0.5 mM thiamine triphosphate
0.048
-
wild type enzyme from supernatant, at 37°C, 50 mM Na-TAPS pH 8.5, 8 mM MgCl2, 0.5 mM thiamine triphosphate
0.09
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 5 mM Na-EDTA
0.45
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 0.04 mM ZnSO4
0.55
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 0.2 mM ZnSO4
0.59
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 4 mM MgCl2 + 4 mM CaCl2
0.63
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 0.1 mM ZnSO4
0.99
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 4 mM MgCl2 + 1 mM CaCl2
1.7
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 4 mM MgCl2
1.9
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 4 mM MgCl2 + 0.1 mM ZnSO4
103
2.55
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 4 mM MgCl2 + 0.04 mM ZnSO4
3.08
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 1 mM MnCl2
3.3
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 0.05 mM MnCl2
3.45
-
K85E-mutated GST-tagged thiamine triphosphatase, pH 8.2, in the presence of 0.1 mM MnCl2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
8.5
9.4
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
about 55% of maximal activity at pH 5.0 and pH 8.0, membrane-associated enzyme
7 - 9.5
-
pH 7.0: about 60% of maximal activity, pH 9.5: about 75% of maximal activity
7.5 - 9.5
-
pH 7.5: about 30% of maximal activity, pH 9.5: about 50% of maximal activity
8 - 10
-
pH 8.0: about 60% of maximal activity, pH 10.0: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
210006, 210007, 210008, 210009, 210010, 210011, 210013, 210014, 210015, 210016, 210017, 210018, 655198
brenda
-
highest activity in hippocampal pyramidal neurons, as well as cerbellar granule cells and Purkinje cells. Some interneurons are also labeled and many thiamine triphosphatase mRNA-positive and immunoreactive cells are distributed thoughout cerebral cortical gray matter and the thalamus. No significant activity in white matter
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (487 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23892
25000
27000
29100
33900
additional information
25000
x * 25000, enzyme solution structure determination by NMR spectroscopy, binding of Mg2+ induces only a minor local conformational change, whereas ThTP binding causes a more global conformational change, structural model for the mThTPase-ThTP-Mg2+ ternary complex, free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold, PDB ID 2JMU, overview
additional information
-
molecular weight of enzyme from brain and pectoralis muscle is above 80000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 25000, enzyme solution structure determination by NMR spectroscopy, binding of Mg2+ induces only a minor local conformational change, whereas ThTP binding causes a more global conformational change, structural model for the mThTPase-ThTP-Mg2+ ternary complex, free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold, PDB ID 2JMU, overview
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.1 M Tris (pH 9.0), 0.2 M MgCl2
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
additional information
overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
at pH 5.0: 50% loss of activity after 83 min, at pH 7.6: about 50% loss of activity after 10 min
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the precipitate treatment with 1% (v/v) sodium deoxycholate causes about 53% solubilization of the enzyme activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MagneGST Protein Purification System, only mutated enzymes expressed as GST fusion proteins
MagneGST Protein Purification System, only mutated enzymes expressed as GST fusion proteins
-
MagneGST Protein Purification System, only mutated enzymes expressed as GST fusion proteins
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21
expression analysis
expression in Escherichia coli, the recombinant enzyme is completely functional
-
overexpression in Escherichia coli as a glutathione S-transferase fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barchi, R.L.; Braun, P.E.
A membrane-associated thiamine triphosphatase from rat brain. Properties of the enzyme
J. Biol. Chem.
247
7668-7673
1972
Rattus norvegicus
brenda
Hashitani, Y.; Cooper, J.R.
The partial purification of thiamine triphosphatase from rat brain
J. Biol. Chem.
247
2117-2119
1972
Rattus norvegicus
brenda
Barchi, R.L.; Braun, P.E.
Thiamine triphosphatase in the nervous system
Biochim. Biophys. Acta
255
402-405
1972
Rattus norvegicus
brenda
Iwata, H.; Baba, A.; Matsuda, T.; Terashita, Z.; Ishii, K.
Role of thiamine metabolism in the central nervous system. II. Effects of various agents on thiamine triphosphatase activity in rat brain
Jpn. J. Pharmacol.
24
825-829
1974
Rattus norvegicus
brenda
Iwata, H.; Baba, A.; Matsuda, T.
Role of thiamine metabolism in the central nervous system. I. Basic properties of thiamine triphosphatase in rat brain
Jpn. J. Pharmacol.
24
817-823
1974
Rattus norvegicus
brenda
Iwata, H.; Baba, A.; Matsuda, T.; Terashita, Z.
Properties of thiamine di- and triphosphatases in rat brain microsomes: effects of chlorpromazine
J. Neurochem.
24
1209-1213
1975
Rattus norvegicus
brenda
Matsuda, T.; Tonomura, H.; Baba, A.; Iwata, H.
Membrane-associated thiamine triphosphatase in rat skeletal muscle
Int. J. Biochem.
23
1111-1114
1991
Rattus norvegicus
brenda
Barchi, R.L.; Viale, R.O.
Membrane-associated thiamin triphosphatase. II. Activation by divalent cations
J. Biol. Chem.
251
193-197
1976
Rattus norvegicus
brenda
Barchi, R.L.
Membrane thiamine triphosphatase from rat brain: inhibition by ATP and ADP
J. Neurochem.
26
715-720
1976
Rattus norvegicus
brenda
Iwata, H.; Baba, A.; Matsuda, T.; Terashita, Z.
Some properties of the enzyme system degrading phosphorylated thiamines in the brain and the effect of chlorpromazine
Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)
2. Meeting
213-221
1974
Rattus norvegicus
-
brenda
Barchi, R.L.
Thiamine triphosphatases in brain
Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)
195-212
1974
Rattus norvegicus
-
brenda
Penttinen, H.K.; Uotila, L.
The relation of the soluble thiamine triphosphatase activity of various rat tissues to nonspecific phosphatases
Med. Biol.
59
177-184
1981
Rattus norvegicus
brenda
Ogawa, K.; Sakai, M.
Recent findings on ultracytochemistry of thiamin phosphatases
Ann. N. Y. Acad. Sci.
378
188-214
1982
Rattus norvegicus
brenda
Nishimune, T.; Hayashi, R.
Hydrolysis and synthesis of thiamin triphosphate in bacteria
J. Nutr. Sci. Vitaminol.
33
113-127
1987
Aneurinibacillus aneurinilyticus, Escherichia coli, Escherichia coli W 1485
brenda
Makarchikov, A.F.; Chernikevich, I.P.
Purification and characterization of thiamine triphosphatase from bovine brain
Biochim. Biophys. Acta
1117
326-332
1992
Bos taurus
brenda
Bettendorff, L.; Mastrogiacomo, F.; Kish, S.J.; Grisar, T.
Thiamine, thiamine phosphates, and their metabolizing enzymes in human brain
J. Neurochem.
66
250-258
1996
Homo sapiens
brenda
Bettendorff, L.; Longree, I.; Wins, P.; Schoffeniels, E.
Solubilization and thiamine triphosphatase from the electric organ of Electrophorus electricus
Biochim. Biophys. Acta
1073
69-76
1991
Electrophorus electricus
brenda
Makarchikov, A.F.; Chernikevich, I.P.
Thiamine triphosphatase activity in bovine kidney
Biochem. Mol. Biol. Int.
46
115-123
1998
Bos taurus
brenda
Bettendorff, L.
Application of high-performance liquid chromatography to the study of thiamine metabolism and in particular thiamine triphosphatase
J. Chromatogr.
566
397-408
1991
Electrophorus electricus
brenda
Makarchikov, A.F.; Lakaye, B.; Gulyai, I.E.; Czerniecki, J.; Coumans, B.; Wins, P.; Grisar, T.; Bettendorff, L.
Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals
Cell. Mol. Life Sci.
60
1477-1488
2003
Bos taurus, Gallus gallus, Homo sapiens, quail, Rattus norvegicus, Sus scrofa
brenda
Lakaye, B.; Makarchikov, A.F.; Wins, P.; Margineanu, I.; Roland, S.; Lins, L.; Aichour, R.; Lebeau, L.; El Moualij, B.; Zorzi, W.; Coumans, B.; Grisar, T.; Bettendorff, L.
Human recombinant thiamine triphosphatase: purification, secondary structure and catalytic properties
Int. J. Biochem. Cell Biol.
36
1348-1364
2004
Homo sapiens
brenda
Lakaye, B.; Makarchikov, A.F.; Antunes, A.F.; Zorzi, W.; Coumans, B.; De Pauw, E.; Wins, P.; Grisar, T.; Bettendorff, L.
Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues
J. Biol. Chem.
277
13771-13777
2002
Bos taurus (Q8MKF1), Bos taurus, Homo sapiens (Q9BU02), Homo sapiens
brenda
Czerniecki, J.; Chanas, G.; Verlaet, M.; Bettendorff, L.; Makarchikov, A.F.; Leprince, P.; Wins, P.; Grisar, T.; Lakaye, B.
Neuronal localization of the 25-kDa specific thiamine triphosphatase in rodent brain
Neuroscience
125
833-840
2004
Rattus norvegicus
brenda
Szyniarowski Piot, S.P.; Lakaye Bernar, L.B.; Czerniecki Ja, C.J.; Makarchikov Alexander , M.A.; Wins Pierr, W.P.; Margineanu Ilc, M.I.; Coumans Bernar, C.B.; Grisar Thierr, G.T.; Bettendorff Lucie, B.L.
Pig tissues express a catalytically inefficient 25-kDa thiamine triphosphatase: insight in the catalytic mechanisms of this enzyme
Biochim. Biophys. Acta
1725
93-102
2005
Sus scrofa, Homo sapiens (Q9BU02), Homo sapiens
brenda
Lakaye, B.; Verlaet, M.; Dubail, J.; Czerniecki, J.; Bontems, S.; Makarchikov, A.F.; Wins, P.; Piette, J.; Grisar, T.; Bettendorff, L.
Expression of 25 kDa thiamine triphosphatase in rodent tissues using quantitative PCR and characterization of its mRNA
Int. J. Biochem. Cell Biol.
36
2032-2041
2004
Rattus norvegicus, Mus musculus (Q8JZL3), Mus musculus
brenda
Song, J.; Bettendorff, L.; Tonelli, M.; Markley, J.L.
Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase
J. Biol. Chem.
283
10939-10948
2008
Mus musculus (Q8JZL3), Mus musculus
brenda
Kovacevic, Z.; Fu, D.; Richardson, D.R.
The iron-regulated metastasis suppressor, Ndrg-1: identification of novel molecular targets
Biochim. Biophys. Acta
1783
1981-1992
2008
Homo sapiens, Rattus norvegicus (Q8CGV7)
brenda
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.
Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase
Biochim. Biophys. Acta
1830
4513-4523
2013
Mus musculus (Q8JZL3), Homo sapiens (Q9BU02)
brenda
Martinez, J.; Truffault, V.; Hothorn, X.
Structural determinants for substrate binding and catalysis in triphosphate tunnel metalloenzymes
J. Biol. Chem.
290
23348-23360
2015
Mus musculus (Q8JZL3)
brenda
Kolas, I.; Makarchikov, A.
Properties of chicken liver membrane-associated thiamine triphosphatase
Ukr. Biochem. J.
87
37-46
2015
Gallus gallus
brenda
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