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Literature summary extracted from

  • Song, J.; Bettendorff, L.; Tonelli, M.; Markley, J.L.
    Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase (2008), J. Biol. Chem., 283, 10939-10948.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.28 Ca2+ Ca2+ inhibits hThTPase activity through competition with Mg2+ Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.28 additional information
-
 additional information kinetics Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.28 cytosol
-
 Mus musculus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.28 Mg2+ the enzyme has an absolute requirement for divalent cations, binding of Mg2+ induces only a minor local conformational change Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.28 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 Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.28 thiamine triphosphate + H2O Mus musculus
-
 thiamine diphosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.28 Mus musculus Q8JZL3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.28 thiamine triphosphate + H2O = thiamine diphosphate + phosphate catalytic mechanism Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.28 thiamine triphosphate + H2O
-
 Mus musculus thiamine diphosphate + phosphate
-
 ?
3.6.1.28 thiamine triphosphate + H2O 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 Mus musculus thiamine diphosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.28 ? 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 Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.6.1.28 ThTPase
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.28 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.28 8.3
-
 assay at Mus musculus