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Literature summary for 3.6.1.28 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

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

KM Value [mM]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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)

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

Organism

Organism UniProt Comment Textmining
Mus musculus Q8JZL3
-
-

Reaction

Reaction Comment Organism Reaction ID
thiamine triphosphate + H2O = thiamine diphosphate + phosphate catalytic mechanism Mus musculus

Substrates and Products (Substrate)

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

Subunits Comment Organism
? 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

Synonyms Comment Organism
ThTPase
-
Mus musculus

Temperature Optimum [°C]

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

pH Optimum

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