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EC Tree
The taxonomic range for the selected organisms is: Homo sapiens 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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25-kDa thiamine triphosphatase
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phosphatase, thiamine tri-
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thiamine triphosphatase
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thiamine triphosphatase
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Thtpa
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ThTPase
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phosphoric ester hydrolysis
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thiamine-triphosphate phosphohydrolase
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ATP + H2O
ADP + phosphate
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the catalytic efficiency is about 4 orders of magnitude lower than for thiamine triphosphate
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?
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
additional information
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Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
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thiamine triphosphate + H2O
thiamine diphosphate + phosphate
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thiamine triphosphate + H2O
thiamine diphosphate + phosphate
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thiamine triphosphate + H2O
thiamine diphosphate + phosphate
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thiamine triphosphate + H2O
thiamine diphosphate + phosphate
absolute specificity
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additional information
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Thtpa is known to decrease the levels of the energy currency molecule, thiamine triphosphate
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?
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Mg2+
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required
Mg2+
enzyme is 5% active in the absence of Mg2+
Zn2+
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inhibits at micromolar concentrations at pH 8.0, activates at pH 6.0
Zn2+
in the presence of Mg2+ at pH 8
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([2-[3-(4-Amino-2-methyl-pyrimidin-5-ylmethyl)-4-methyl-thiazol-5-yl]-ethoxy]-phosphonomethyl-phosphinoylmethyl)-phosphonic acid
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5,5'-dithiobis-2-nitrobenzoic acid
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ATP
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very poor inhibitor
SDS
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IC50: about 0.3% W/v. The inhibition is partially reversible, probably due to correct refolding of the denatured enzyme
thiamine triphosphate
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Ca2+
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inhibits by competition with Mg2+
Zn2+
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inhibits at micromolar concentrations at pH 8.0, IC50: about 0.015-0.02 mM. Activates at pH 6.0
Zn2+
pH 8.5, IC50: 0.007 mM
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additional information
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overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
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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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3.7
ATP
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in presence of 8 mM ATP
0.126
thiamin triphosphate
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0.056 - 0.25
thiamine triphosphate
0.056
thiamine triphosphate
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0.126
thiamine triphosphate
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0.15
thiamine triphosphate
wild type enzyme
0.154
thiamine triphosphate
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untagged recombinant enzyme
0.25
thiamine triphosphate
GST-fused E63Q mutant enzyme
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0.24
ATP
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in presence of 8 mM Mg2+
140 - 240
thiamine triphosphate
140
thiamine triphosphate
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240
thiamine triphosphate
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1.2
([2-[3-(4-Amino-2-methyl-pyrimidin-5-ylmethyl)-4-methyl-thiazol-5-yl]-ethoxy]-phosphonomethyl-phosphinoylmethyl)-phosphonic acid
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0.95
thiamine triphosphate
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0.03
Ca2+
GST-fused E78K mutant enzyme
0.15
Ca2+
GST-fused wild type enzyme
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0.007
Zn2+
Homo sapiens
pH 8.5, IC50: 0.007 mM
0.015 - 0.02
Zn2+
Homo sapiens
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inhibits at micromolar concentrations at pH 8.0, IC50: about 0.015-0.02 mM. Activates at pH 6.0
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140
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purified recombinant enzyme
225
pure untagged recombinant thiamine triphosphatase, 37°C, pH 8.2
4.5
wild type thiamine triphosphatase from supernatant
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9.4
GST-fused E63Q mutant enzyme
8.5
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7 - 9.5
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pH 7.0: about 60% of maximal activity, pH 9.5: about 75% of maximal activity
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brenda
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SwissProt
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SwissProt
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non-metastatic human colorectal adenocarcinoma cells
brenda
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brenda
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brenda
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metastatic lung cancer cells
brenda
high activity
brenda
high activity
brenda
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brenda
high activity
brenda
low activity
brenda
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cerebral cortex
brenda
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brenda
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THTPA_HUMAN
230
0
25566
Swiss-Prot
other Location (Reliability: 1 )
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23892
1 * 23892, mass spectrometry
27000
1 * 27000, SDS-PAGE
25000
gel filtration
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monomer
1 * 27000, SDS-PAGE
monomer
1 * 23892, mass spectrometry
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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
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additional information
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overexpression of N-myc downstream regulated gene-1, Ndrg-1, leads to upregulation of Thtpa in cancer cells, overview
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5
GST-tagged wild type enzyme activity was nearly zero at pH 5.0
68
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30 min, 50% loss of activity
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MagneGST Protein Purification System, only mutated enzymes expressed as GST fusion proteins
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expressed in Escherichia coli strain BL21
expression in Escherichia coli, the recombinant enzyme is completely functional
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overexpression in Escherichia coli as a glutathione S-transferase fusion protein
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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
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
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
Homo sapiens (Q9BU02), Homo sapiens, Sus scrofa
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