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Literature summary for 2.4.2.7 extracted from
- Cloning, expression and biochemical characterization of xanthine and adenine phosphoribosyltransferases from Thermus thermophilus HB8 (2018), Biocatal. Biotransform., 36, 216-223 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aprt2, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Thermus thermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Thermus thermophilus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
analytical ultracentrifugation analysis | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus | - |
AMP + diphosphate | - |
r | |
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus DSM 579 | - |
AMP + diphosphate | - |
r | |
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus ATCC 27634 | - |
AMP + diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q5SHW6 | - |
- |
| Thermus thermophilus ATCC 27634 | Q5SHW6 | - |
- |
| Thermus thermophilus DSM 579 | Q5SHW6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatement, nickel affinity chromatography, and gel filtration | Thermus thermophilus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Thermus thermophilus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.32 | - |
purified recombinant enzyme, pH 8.5, 70°C, substrate adenine | Thermus thermophilus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20--80°C, purified recombinant His-tagged enzyme, 70-80% activity reamining after 70 days | Thermus thermophilus |
| 4°C, purified recombinant His-tagged enzyme, 85% activity remaining after 70 days | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | AMP + diphosphate | - |
r | |
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | AMP + diphosphate | - |
r | |
| adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | AMP + diphosphate | - |
r | |
| additional information | substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2 | Thermus thermophilus | ? | - |
- |
|
| additional information | substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2 | Thermus thermophilus DSM 579 | ? | - |
- |
|
| additional information | substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2 | Thermus thermophilus ATCC 27634 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 19150, about, sequence calculation, 2 * 21000, His-tagged recombinant enzyme TtAPRT2, SDS-PAGE | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| APRT2 | - |
Thermus thermophilus |
| TtAPRT2 | - |
Thermus thermophilus |
| TTHA1614 | locus name | Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
recombinant enzyme | Thermus thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 90 | and above, activity range, profile overview. Recombinant enzyme displays a strong temperature dependence with over 75% of relative activity at 70-90°C | Thermus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
recombinant enzyme | Thermus thermophilus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 10 | activity range, recombinant enzyme, highest activity at pH 8.0-10.0, profile overview | Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+ | Thermus thermophilus |
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