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Literature summary extracted from
- Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5-deoxy-5-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus (2011), Biochim. Biophys. Acta, 1814, 1358-1366.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.4.2.28 | expressed in Escherichia coli | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.2.28 | Pyrococcus furiosus | Q8U4Q8 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.2.28 | additional information | PfMTAP is characterized by a broad substrate specificity towards purine nucleosides, with a 20fold higher catalytic efficacy for adenosine and 5'-methylthioadenosine than for inosine and guanosine | Pyrococcus furiosus | ? | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.2.28 | 5'-deoxy-5'-methylthioadenosine phosphorylase | - |
Pyrococcus furiosus |
| 2.4.2.28 | PfMTAP | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.2.28 | 80 | - |
assay at | Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.2.28 | additional information | - |
PfMTAP is a highly thermostable protein | Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.2.28 | 7.4 | - |
assay at | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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