Cloned (Comment) | Organism |
---|---|
gene xprt, 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Thermus thermophilus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
analytical ultracentrifugation analysis | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus | - |
XMP + diphosphate | - |
r | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus DSM 579 | - |
XMP + diphosphate | - |
r | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus ATCC 27634 | - |
XMP + diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q5SKV8 | - |
- |
Thermus thermophilus ATCC 27634 | Q5SKV8 | - |
- |
Thermus thermophilus DSM 579 | Q5SKV8 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatement, nickel affinity chromatography, and gel filtration | Thermus thermophilus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.1 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate guanine | Thermus thermophilus |
0.12 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate hypoxanthine | Thermus thermophilus |
1.7 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate xanthine | Thermus thermophilus |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | GMP + diphosphate | - |
r | |
guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | GMP + diphosphate | - |
r | |
guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | GMP + diphosphate | - |
r | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus | IMP + diphosphate | - |
r | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus DSM 579 | IMP + diphosphate | - |
r | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus ATCC 27634 | IMP + diphosphate | - |
r | |
additional information | substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine | Thermus thermophilus | ? | - |
- |
|
additional information | substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine | Thermus thermophilus DSM 579 | ? | - |
- |
|
additional information | substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine | Thermus thermophilus ATCC 27634 | ? | - |
- |
|
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | XMP + diphosphate | - |
r | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | XMP + diphosphate | - |
r | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | XMP + diphosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 17100, calculated from amino acid sequence | Thermus thermophilus |
homotetramer | 4 * 19020, about, sequence calculation, 4 * 19000, His-tagged recombinant enzyme TtXPRT, SDS-PAGE | Thermus thermophilus |
Synonyms | Comment | Organism |
---|---|---|
ttha0535 | - |
Thermus thermophilus |
TtXPRT | - |
Thermus thermophilus |
xanthine phosphoribosyltransferase | - |
Thermus thermophilus |
XPRT | - |
Thermus thermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
recombinant enzyme | Thermus thermophilus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 90 | and above, activity range, profile overview. Recombinant enzyme displays a strong temperature dependence with over 75% of relative activity at 60-90°C | Thermus thermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant enzyme | Thermus thermophilus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 8.5 | activity range, recombinant enzyme, highest activity at pH 5.0-6.0, profile overview | Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
evolution | conserved XPRT PRPP motif sequence comparisons | Thermus thermophilus |
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 |