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Literature summary for 3.6.1.66 extracted from
- Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii (2001), Nucleic Acids Res., 29, 3099-3107.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
- |
Archaeoglobus fulgidus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.22 | - |
XTP | pH 10.5, 80°C | Methanocaldococcus jannaschii |  |
| 0.24 | - |
ITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
| 0.25 | - |
dITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | the enzyme requires a divalent cation. Mg2+ is required for optimal activity, with Mn2+, Zn2+ and Ni2+ supporting less than 50% of the maximum rate | Methanocaldococcus jannaschii | |
| Ni2+ | the enzyme requires a divalent cation. Mg2+ is required for optimal activity, with Mn2+, Zn2+ and Ni2+ supporting less than 50% of the maximum rate | Methanocaldococcus jannaschii | |
| Zn2+ | the enzyme requires a divalent cation. Mg2+ is required for optimal activity, with Mn2+, Zn2+ and Ni2+ supporting less than 50% of the maximum rate | Methanocaldococcus jannaschii | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dITP + H2O | Methanocaldococcus jannaschii | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | dIMP + diphosphate | - |
? | |
| dITP + H2O | Methanocaldococcus jannaschii DSM 2661 | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | dIMP + diphosphate | - |
? | |
| XTP + H2O | Methanocaldococcus jannaschii | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | XMP + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O28046 | - |
- |
| Escherichia coli | - |
- |
- |
| Methanocaldococcus jannaschii | Q57679 | - |
- |
| Methanocaldococcus jannaschii DSM 2661 | Q57679 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
- |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dITP + H2O | - |
Escherichia coli | dIMP + diphosphate | - |
? | |
| dITP + H2O | - |
Archaeoglobus fulgidus | dIMP + diphosphate | - |
? | |
| dITP + H2O | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | Methanocaldococcus jannaschii | dIMP + diphosphate | - |
? | |
| dITP + H2O | i.e. 2'-deoxyinosine 5'-triphosphate | Methanocaldococcus jannaschii | dIMP + diphosphate | - |
? | |
| dITP + H2O | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | Methanocaldococcus jannaschii DSM 2661 | dIMP + diphosphate | - |
? | |
| dITP + H2O | i.e. 2'-deoxyinosine 5'-triphosphate | Methanocaldococcus jannaschii DSM 2661 | dIMP + diphosphate | - |
? | |
| ITP + H2O | - |
Methanocaldococcus jannaschii | IMP + diphosphate | - |
? | |
| ITP + H2O | - |
Methanocaldococcus jannaschii DSM 2661 | IMP + diphosphate | - |
? | |
| additional information | catalytic efficiency (kcat/Km) is less than 1% compared to dITP or XTP with the following substrates: dGTP, GTP, dATP, dCTP, dTTP, dUTP, 8-oxo-dGTP. Neither endonuclease nor 3'-exonuclease activities were detected in this protein | Methanocaldococcus jannaschii | ? | - |
? | |
| additional information | reaction rate is less than 1% compared to dITP or XTP with the following substrates: dGTP, dATP, dCTP, dTTP, dUTP | Archaeoglobus fulgidus | ? | - |
? | |
| additional information | reaction rate is less than 2% compared to dITP or XTP with the following substrates: dGTP, dATP, dCTP, dTTP, dUTP | Escherichia coli | ? | - |
? | |
| additional information | catalytic efficiency (kcat/Km) is less than 1% compared to dITP or XTP with the following substrates: dGTP, GTP, dATP, dCTP, dTTP, dUTP, 8-oxo-dGTP. Neither endonuclease nor 3'-exonuclease activities were detected in this protein | Methanocaldococcus jannaschii DSM 2661 | ? | - |
? | |
| XTP + H2O | - |
Escherichia coli | XMP + diphosphate | - |
? | |
| XTP + H2O | - |
Methanocaldococcus jannaschii | XMP + diphosphate | - |
? | |
| XTP + H2O | - |
Archaeoglobus fulgidus | XMP + diphosphate | - |
? | |
| XTP + H2O | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | Methanocaldococcus jannaschii | XMP + diphosphate | - |
? | |
| XTP + H2O | - |
Methanocaldococcus jannaschii DSM 2661 | XMP + diphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Af2237 | - |
Archaeoglobus fulgidus |
| Ec197 | - |
Escherichia coli |
| hypoxanthine/xanthine dNTP pyrophosphatase | - |
Methanocaldococcus jannaschii |
| Mj0226 | - |
Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Escherichia coli |
| 80 | - |
- |
Methanocaldococcus jannaschii |
| 80 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 90 | 30°C: about 20% of maximal activity, 90°C: 90% of maximal activity | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability is highest near 300 mM NaCl | Methanocaldococcus jannaschii |
| 83 | - |
irreversible denaturation above | Methanocaldococcus jannaschii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 152.4 | - |
dITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
| 155.8 | - |
ITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
| 176.4 | - |
XTP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
assay at | Escherichia coli |
| 10.5 | - |
assay at | Methanocaldococcus jannaschii |
| 10.5 | - |
assay at | Archaeoglobus fulgidus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA | Methanocaldococcus jannaschii |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 609.8 | - |
dITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
| 649.1 | - |
ITP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
| 801.8 | - |
XTP | pH 10.5, 80°C | Methanocaldococcus jannaschii | |
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