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Literature summary for 3.6.1.73 extracted from
- Identification of an ITPase/XTPase in Escherichia coli by structural and biochemical analysis (2005), Structure, 13, 1511-1520 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| vapor diffusion by hanging drop, crystal structure at 2.25 A resolution | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ATP | competitive | Escherichia coli |  |
| GTP | competitive | Escherichia coli | |
| TTP | competitive | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.5 | - |
inosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 1.17 | - |
xanthosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 1.24 | - |
2'-deoxyinosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 4.51 | - |
guanosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | the enzyme binds 1 divalent cation per subunit. Activity is maximal in the presence of Mg2+. Activity with Mn2+ is 80% compared to activity with Mg2+. Km: 0.91 mM | Escherichia coli | |
| Mn2+ | the enzyme binds 1 divalent cation per subunit. Activity is maximal in the presence of Mg2+. Activity with Mn2+ is 80% compared to activity with Mg2+. KM: 1.39 mM | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| inosine 5'-triphosphate + H2O | Escherichia coli | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | inosine 5'-diphosphate + phosphate | - |
? | |
| inosine 5'-triphosphate + H2O | Escherichia coli K12 | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | inosine 5'-diphosphate + phosphate | - |
? | |
| xanthosine 5'-triphosphate + H2O | Escherichia coli | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | xanthosine 5'-diphosphate + phosphate | - |
? | |
| xanthosine 5'-triphosphate + H2O | Escherichia coli K12 | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | xanthosine 5'-diphosphate + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P39411 | - |
- |
| Escherichia coli K12 | P39411 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2'-deoxyinosine 5'-triphosphate + H2O | - |
Escherichia coli | 2'-deoxyinosine 5'-diphosphate + phosphate | - |
? | |
| guanosine 5'-triphosphate + H2O | - |
Escherichia coli | guanosine 5'-diphosphate + phosphate | - |
? | |
| inosine 5'-triphosphate + H2O | - |
Escherichia coli | inosine 5'-diphosphate + phosphate | - |
? | |
| inosine 5'-triphosphate + H2O | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | Escherichia coli | inosine 5'-diphosphate + phosphate | - |
? | |
| inosine 5'-triphosphate + H2O | - |
Escherichia coli K12 | inosine 5'-diphosphate + phosphate | - |
? | |
| inosine 5'-triphosphate + H2O | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | Escherichia coli K12 | inosine 5'-diphosphate + phosphate | - |
? | |
| additional information | the enzyme is not active on dATP and dGTP, and exhibits no phosphatase activity toward pyrimidines (CTP, TTP, UTP, dCTP, and dTTP) | Escherichia coli | ? | - |
? | |
| additional information | the enzyme is not active on dATP and dGTP, and exhibits no phosphatase activity toward pyrimidines (CTP, TTP, UTP, dCTP, and dTTP) | Escherichia coli K12 | ? | - |
? | |
| xanthosine 5'-triphosphate + H2O | - |
Escherichia coli | xanthosine 5'-diphosphate + phosphate | - |
? | |
| xanthosine 5'-triphosphate + H2O | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | Escherichia coli | xanthosine 5'-diphosphate + phosphate | - |
? | |
| xanthosine 5'-triphosphate + H2O | - |
Escherichia coli K12 | xanthosine 5'-diphosphate + phosphate | - |
? | |
| xanthosine 5'-triphosphate + H2O | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | Escherichia coli K12 | xanthosine 5'-diphosphate + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ITPase/XTPase | - |
Escherichia coli |
| yjjX | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 22.3 | - |
2'-deoxyinosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 573.3 | - |
inosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 616.5 | - |
guanosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 2625 | - |
xanthosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.75 | - |
- |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 18 | - |
2'-deoxyinosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 136.4 | - |
guanosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 1147 | - |
inosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
| 2243 | - |
xanthosine 5'-triphosphate | 25°C, pH 6.75 | Escherichia coli | |
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