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Literature summary for 2.4.2.9 extracted from
- Sustainable synthesis of uridine-5-monophosphate analogues by immobilized uracil phosphoribosyltransferase from Thermus thermophilus (2020), Biochim. Biophys. Acta, 1868, 140251 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | MtTtUPRT is successfully applied in the enzymatic synthesis of therapeutic NMP analogues. The immobilized enzyme is usable as a biocatalyst in the synthesis of different 5-modified uridine-5'-monophosphates at short times. MTtUPRT3 can be reused up to 8 times in the synthesis of uridine-5'-monophosphate (UMP) with maximum activity at 100°C and pH 7.0 (activity 968 IU/g support, retaining activity 100%). Potential application of MTtUPRT3 as industrial biocatalyst | Thermus thermophilus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of N-terminal His6-tagged TtUPRT | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | covalent immobilization of uracil phosphoribosyltransferase (UPRT) from Thermus thermophilus HB8 onto glutaraldehyde-activated magnetic iron oxide porous microparticles (MTtUPRT). The support is activated by contacting the microspheres with 0.2 ml of 50 mM sodium phosphate buffer, pH 8.5, containing 5% w/v glutaraldehyde during 3 h at 25°C, and then washed thoroughly with distilled water to remove the excess activating agent. Finally, activated microspheres are washed and equilibrated in binding buffer (50 mM potassium phosphate buffer, pH 8.5), shortly prior to use. According to the catalyst load experiments, MTtUPRT3 is selected as optimal biocatalyst. MTtUPRT3 is active and stable in a broad range of temperature (70-100°C) and in the pH interval 6.0-8.0, displaying maximum activity at 100°C and pH 7.0 (activity 968 IU/g support, retaining activity 100%). In addition, MTtUPRT3 can be reused up to 10 times in the synthesis of uridine-5'-monophosphate (UMP), completely stable for 6 cycles. Biocatalyst recycling is studied by employing MTtUPRT3 in consecutive reactions. MTtUPRT3 is successfully applied in the sustainable synthesis of different 5-modified uridine-5'-monophosphates at short times | Thermus thermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required for catalysis | Thermus thermophilus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UMP + diphosphate | Thermus thermophilus | - |
uracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q5SIQ7 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-bromo-UMP + diphosphate | - |
Thermus thermophilus | 5-bromouracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| 5-chloro-UMP + diphosphate | - |
Thermus thermophilus | 5-chlorouracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| 5-fluoro-UMP + diphosphate | - |
Thermus thermophilus | 5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| 5-iodo-UMP + diphosphate | - |
Thermus thermophilus | 5-iodouracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| UMP + diphosphate | - |
Thermus thermophilus | uracil + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | structure modeling, overview | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TtUPRT | - |
Thermus thermophilus |
| TtUPRT3 | - |
Thermus thermophilus |
| UPP | - |
Thermus thermophilus |
| UPRT | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
free enzyme | Thermus thermophilus |
| 100 | - |
immobilized enzyme | Thermus thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 100 | over 40% of maximal activity within this range, profile overview | Thermus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
immobilized enzyme | Thermus thermophilus |
| 8 | - |
free enzyme | Thermus thermophilus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | over 60% of maximal activity within this range, profile overview | Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | uracil phosphoribosyltransferase (UPRT) catalyzes the reversible transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl1-diphosphate (PRPP) to uracil N1 to form uridine-5'-monophosphate, UMP, in the presence of Mg2+. Nucleosides are essential metabolites in numerous biochemical processes in all living organisms | Thermus thermophilus |
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