EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.2.7 | 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 |
2.4.2.22 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.2.7 | Mg2+ | required | Thermus thermophilus | |
2.4.2.22 | Mg2+ | required | Thermus thermophilus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | additional information | - |
analytical ultracentrifugation analysis | Thermus thermophilus |
2.4.2.22 | additional information | - |
analytical ultracentrifugation analysis | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus | - |
AMP + diphosphate | - |
r | |
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus DSM 579 | - |
AMP + diphosphate | - |
r | |
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus ATCC 27634 | - |
AMP + diphosphate | - |
r | |
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus | - |
XMP + diphosphate | - |
r | |
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus DSM 579 | - |
XMP + diphosphate | - |
r | |
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus ATCC 27634 | - |
XMP + diphosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.2.7 | Thermus thermophilus | Q5SHW6 | - |
- |
2.4.2.7 | Thermus thermophilus ATCC 27634 | Q5SHW6 | - |
- |
2.4.2.7 | Thermus thermophilus DSM 579 | Q5SHW6 | - |
- |
2.4.2.22 | Thermus thermophilus | Q5SKV8 | - |
- |
2.4.2.22 | Thermus thermophilus ATCC 27634 | Q5SKV8 | - |
- |
2.4.2.22 | Thermus thermophilus DSM 579 | Q5SKV8 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.2.7 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatement, nickel affinity chromatography, and gel filtration | Thermus thermophilus |
2.4.2.22 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatement, nickel affinity chromatography, and gel filtration | Thermus thermophilus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.4.2.7 | commercial preparation | - |
Thermus thermophilus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | 0.32 | - |
purified recombinant enzyme, pH 8.5, 70°C, substrate adenine | Thermus thermophilus |
2.4.2.22 | 0.1 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate guanine | Thermus thermophilus |
2.4.2.22 | 0.12 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate hypoxanthine | Thermus thermophilus |
2.4.2.22 | 1.7 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate xanthine | Thermus thermophilus |
EC Number | Storage Stability | Organism |
---|---|---|
2.4.2.7 | -20--80°C, purified recombinant His-tagged enzyme, 70-80% activity reamining after 70 days | Thermus thermophilus |
2.4.2.7 | 4°C, purified recombinant His-tagged enzyme, 85% activity remaining after 70 days | Thermus thermophilus |
2.4.2.22 | -20--80°C, purified recombinant His-tagged enzyme, 70-80% activity reamining after 70 days | Thermus thermophilus |
2.4.2.22 | 4°C, purified recombinant His-tagged enzyme, 85% activity remaining after 70 days | Thermus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | AMP + diphosphate | - |
r | |
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | AMP + diphosphate | - |
r | |
2.4.2.7 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | AMP + diphosphate | - |
r | |
2.4.2.7 | 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 | ? | - |
- |
|
2.4.2.7 | 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 | ? | - |
- |
|
2.4.2.7 | 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 | ? | - |
- |
|
2.4.2.22 | guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | GMP + diphosphate | - |
r | |
2.4.2.22 | guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | GMP + diphosphate | - |
r | |
2.4.2.22 | guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | GMP + diphosphate | - |
r | |
2.4.2.22 | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus | IMP + diphosphate | - |
r | |
2.4.2.22 | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus DSM 579 | IMP + diphosphate | - |
r | |
2.4.2.22 | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | reaction of EC 2.4.2.8 | Thermus thermophilus ATCC 27634 | IMP + diphosphate | - |
r | |
2.4.2.22 | 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 | ? | - |
- |
|
2.4.2.22 | 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 | ? | - |
- |
|
2.4.2.22 | 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 | ? | - |
- |
|
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | XMP + diphosphate | - |
r | |
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 579 | XMP + diphosphate | - |
r | |
2.4.2.22 | xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC 27634 | XMP + diphosphate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.2.7 | homodimer | 2 * 19150, about, sequence calculation, 2 * 21000, His-tagged recombinant enzyme TtAPRT2, SDS-PAGE | Thermus thermophilus |
2.4.2.22 | homotetramer | 4 * 17100, calculated from amino acid sequence | Thermus thermophilus |
2.4.2.22 | homotetramer | 4 * 19020, about, sequence calculation, 4 * 19000, His-tagged recombinant enzyme TtXPRT, SDS-PAGE | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.2.7 | APRT2 | - |
Thermus thermophilus |
2.4.2.7 | TtAPRT2 | - |
Thermus thermophilus |
2.4.2.7 | TTHA1614 | locus name | Thermus thermophilus |
2.4.2.22 | ttha0535 | - |
Thermus thermophilus |
2.4.2.22 | TtXPRT | - |
Thermus thermophilus |
2.4.2.22 | xanthine phosphoribosyltransferase | - |
Thermus thermophilus |
2.4.2.22 | XPRT | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | 70 | - |
recombinant enzyme | Thermus thermophilus |
2.4.2.22 | 70 | - |
recombinant enzyme | Thermus thermophilus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | 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 |
2.4.2.22 | 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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | 8.5 | - |
recombinant enzyme | Thermus thermophilus |
2.4.2.22 | 6 | - |
recombinant enzyme | Thermus thermophilus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.4.2.7 | 5 | 10 | activity range, recombinant enzyme, highest activity at pH 8.0-10.0, profile overview | Thermus thermophilus |
2.4.2.22 | 4 | 8.5 | activity range, recombinant enzyme, highest activity at pH 5.0-6.0, profile overview | Thermus thermophilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.2.7 | 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 |
2.4.2.22 | evolution | conserved XPRT PRPP motif sequence comparisons | Thermus thermophilus |
2.4.2.22 | 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 |