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Literature summary extracted from
- CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis (2010), Genes Genet. Syst., 85, 287-295.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.1.55 | expression in Escherichia coli CC101 mttT mutant | Ciona intestinalis |
| 3.6.1.55 | expression in Escherichia coli mutT mutant. CiMutT significantly suppressed the mutator activity of Escherichia coli mutT mutant | Ciona intestinalis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.55 | 0.0169 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.55 | Mg2+ | required, optimal activity at 5 mM | Ciona intestinalis | |
| 3.6.1.55 | Mg2+ | 5 mM required for optimal activity | Ciona intestinalis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 20400 | - |
gel filtration | Ciona intestinalis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.55 | 8-oxo-dGTP + H2O | Ciona intestinalis | - |
8-oxo-dGMP + diphosphate | - |
? | |
| 3.6.1.55 | 8-oxo-dGTP + H2O | Ciona intestinalis | the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis | 8-oxo-dGMP + diphosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.1.55 | Ciona intestinalis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.1.55 | - |
Ciona intestinalis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 11.8 | - |
pH 9.5, 30°C, 8-oxo-dGTP | Ciona intestinalis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.55 | 8-oxo-dGTP + H2O | - |
Ciona intestinalis | 8-oxo-dGMP + diphosphate | - |
? | |
| 3.6.1.55 | 8-oxo-dGTP + H2O | the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis | Ciona intestinalis | 8-oxo-dGMP + diphosphate | - |
? | |
| 3.6.1.55 | 8-oxo-dGTP + H2O | the specific activity for 8-oxo-dGTP is greater than that for unoxidized dATP and dGTP | Ciona intestinalis | 8-oxo-dGMP + diphosphate | - |
? | |
| 3.6.1.55 | additional information | in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP | Ciona intestinalis | ? | - |
? | |
| 3.6.1.55 | additional information | no hydrolysis of 2-hydroxy-dATP, 8-oxo-dGDP and 2-oxo-dAMP. The enzyme oxidizes all four unoxidized nucleoside triphosphates with a preference for dATP | Ciona intestinalis | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.1.55 | 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase | - |
Ciona intestinalis |
| 3.6.1.55 | 8-oxo-dGTP diphosphatase | - |
Ciona intestinalis |
| 3.6.1.55 | CiMutT | CiMutT is a functional homologue of Escherichia coli MutT | Ciona intestinalis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 30 | - |
- |
Ciona intestinalis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 20 | 38 | 20°C: about 50% of maximal activity, 38°C: about 80% of maximal activity | Ciona intestinalis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.55 | 2.55 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 9.5 | - |
- |
Ciona intestinalis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.55 | 8.5 | 10.5 | pH 8.5: about 60% of maximal activity, pH 10.5: about 50% of maximal activity | Ciona intestinalis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.1.55 | physiological function | the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis | Ciona intestinalis |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.55 | 15 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis | |
| 3.6.1.55 | 150 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis | |
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