Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli CC101 mttT mutant | Ciona intestinalis |
expression in Escherichia coli mutT mutant. CiMutT significantly suppressed the mutator activity of Escherichia coli mutT mutant | Ciona intestinalis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0169 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, optimal activity at 5 mM | Ciona intestinalis | |
Mg2+ | 5 mM required for optimal activity | Ciona intestinalis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
20400 | - |
gel filtration | Ciona intestinalis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
8-oxo-dGTP + H2O | Ciona intestinalis | - |
8-oxo-dGMP + diphosphate | - |
? | |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Ciona intestinalis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Ciona intestinalis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
11.8 | - |
pH 9.5, 30°C, 8-oxo-dGTP | Ciona intestinalis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
8-oxo-dGTP + H2O | - |
Ciona intestinalis | 8-oxo-dGMP + diphosphate | - |
? | |
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 | - |
? | |
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 | - |
? | |
additional information | in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP | Ciona intestinalis | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase | - |
Ciona intestinalis |
8-oxo-dGTP diphosphatase | - |
Ciona intestinalis |
CiMutT | CiMutT is a functional homologue of Escherichia coli MutT | Ciona intestinalis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
- |
Ciona intestinalis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 38 | 20°C: about 50% of maximal activity, 38°C: about 80% of maximal activity | Ciona intestinalis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.55 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.5 | - |
- |
Ciona intestinalis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8.5 | 10.5 | pH 8.5: about 60% of maximal activity, pH 10.5: about 50% of maximal activity | Ciona intestinalis |
General Information | Comment | Organism |
---|---|---|
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 Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
15 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis | |
150 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis |