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Information on EC 3.6.1.28 - thiamine-triphosphatase and Organism(s) Mus musculus and UniProt Accession Q8JZL3

for references in articles please use BRENDA:EC3.6.1.28
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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.28 thiamine-triphosphatase
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This record set is specific for:
Mus musculus
UNIPROT: Q8JZL3 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 kDa thiamine triphosphatase
-
thiamine triphosphatase
-
phosphatase, thiamine tri-
-
-
-
-
thiamine triphosphatase
-
-
-
-
ThTPase
-
-
-
-
TTPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
thiamine triphosphate + H2O = thiamine diphosphate + phosphate
show the reaction diagram
catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
thiamine-triphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-47-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
thiamine triphosphate + H2O
thiamine diphosphate + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
Ca2+ inhibits hThTPase activity through competition with Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 2.8
thiamine triphosphate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 23
thiamine triphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14 - 8000
thiamine triphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THTPA_MOUSE
224
0
24264
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.1 M Tris (pH 9.0), 0.2 M MgCl2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D147A
about 30% of wild-type catalytic efficiency
D37A
about 0.5% of wild-type catalytic efficiency
E81A
about 30% of wild-type catalytic efficiency
K11A
about 15% of wild-type catalytic efficiency
K193A
about 60% of wild-type catalytic efficiency
K65A
more than 1000fold decrease in kcat value
W53A
2.5fold increase in catalytic efficiency
Y39A
about 30% of wild-type catalytic efficiency
Y79A
about 5% of wild-type catalytic efficiency
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Mus musculus (Q8JZL3), Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team