Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | Ca2+ inhibits hThTPase activity through competition with Mg2+ | Mus musculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Mus musculus | 5829 | - |
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 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
thiamine triphosphate + H2O | Mus musculus | - |
thiamine diphosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q8JZL3 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
thiamine triphosphate + H2O = thiamine diphosphate + phosphate | catalytic mechanism | Mus musculus |
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 | 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 | Comment | Organism |
---|---|---|
ThTPase | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.3 | - |
assay at | Mus musculus |