Any feedback?
Literature summary for 3.6.1.55 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)
| 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 [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0169 | - |
8-oxo-dGTP | pH 9.5, 30°C | Ciona intestinalis |  |
Metals/Ions
| 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 [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 20400 | - |
gel filtration | Ciona intestinalis |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ciona intestinalis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Ciona intestinalis |
Specific Activity [micromol/min/mg]
| 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 and Products (Substrate)
| 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
| 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 [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Ciona intestinalis |
Temperature Range [°C]
| 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 [1/s]
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
- |
Ciona intestinalis |
pH Range
| 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
| 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 [mM/s]
| 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 | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
