EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.B18 | expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
2.7.7.B19 | expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
2.7.7.B20 | expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
2.7.7.23 | expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
2.7.7.24 | expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.23 | additional information | N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C | Sulfurisphaera tokodaii |
2.7.7.24 | additional information | analysis of a deletion mutant lacking the 170-residue C-terminal domain indicated that this region has an important role in the thermostability and activity of the protein. Specific initial velocity (glucose-1-phosphate thymidylyltransferase activity) is 23 times lower than that of the native enzyme when measured at 37°C | Sulfurisphaera tokodaii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.24 | 0.02 | - |
dTTP | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
2.7.7.24 | 0.05 | - |
dTDP-alpha-D-glucose | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
2.7.7.24 | 0.39 | - |
diphosphate | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
2.7.7.24 | 1.12 | - |
alpha-D-glucose 1-phosphate | pH 8.0, 80°C | Sulfurisphaera tokodaii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.23 | Co2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii | |
2.7.7.23 | Mg2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+. The optimal Mg2+ concentration is 6 mM, but the enzymatic activity does not change substantially between 2 and 12 mM | Sulfurisphaera tokodaii | |
2.7.7.23 | Mn2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii | |
2.7.7.23 | Zn2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii | |
2.7.7.24 | Co2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii | |
2.7.7.24 | Mg2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+. The optimal Mg2+ concentration is 6 mM, but the enzymatic activity does not change substantially between 2 and 12 mM | Sulfurisphaera tokodaii | |
2.7.7.24 | Mn2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii | |
2.7.7.24 | Zn2+ | absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ | Sulfurisphaera tokodaii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | Sulfurisphaera tokodaii | - |
diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | Sulfurisphaera tokodaii DSM 16993 | - |
diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
2.7.7.24 | dTTP + alpha-D-glucose 1-phosphate | Sulfurisphaera tokodaii | the enzyme is involved in biosynthesis of L-rhamnose | diphosphate + dTDP-alpha-D-glucose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.B18 | Sulfurisphaera tokodaii | Q975F9 | - |
- |
2.7.7.B18 | Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
2.7.7.B19 | Sulfurisphaera tokodaii | Q975F9 | - |
- |
2.7.7.B19 | Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
2.7.7.B20 | Sulfurisphaera tokodaii | Q975F9 | - |
- |
2.7.7.B20 | Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
2.7.7.23 | Sulfurisphaera tokodaii | Q975F9 | - |
- |
2.7.7.23 | Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
2.7.7.24 | Sulfurisphaera tokodaii | Q975F9 | - |
- |
2.7.7.24 | Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.B18 | - |
Sulfurisphaera tokodaii |
2.7.7.B19 | - |
Sulfurisphaera tokodaii |
2.7.7.B20 | - |
Sulfurisphaera tokodaii |
2.7.7.23 | - |
Sulfurisphaera tokodaii |
2.7.7.24 | - |
Sulfurisphaera tokodaii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.B18 | dGTP + alpha-D-glucose 1-phosphate | activity is 47% compared to the activity with dTTP, cf. EC 2.7.7.24 | Sulfurisphaera tokodaii | diphosphate + dGDP-alpha-D-glucose | - |
? | |
2.7.7.B19 | dGTP + alpha-D-glucose 1-phosphate | activity is 47% compared to the activity with dTTP, cf. EC 2.7.7.24 | Sulfurisphaera tokodaii | diphosphate + dGDP-alpha-D-glucose | - |
? | |
2.7.7.B20 | dATP + alpha-D-glucose 1-phosphate | activity is 40% compared to the activity with dTTP, cf 2.7.7.24 | Sulfurisphaera tokodaii | diphosphate + dADP-alpha-D-glucose | - |
? | |
2.7.7.23 | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
Sulfurisphaera tokodaii | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
Sulfurisphaera tokodaii DSM 16993 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | UTP + alpha-D-glucose 1-phosphate | the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate | Sulfurisphaera tokodaii | diphosphate + UDP-alpha-D-glucose | - |
? | |
2.7.7.23 | UTP + alpha-D-glucose 1-phosphate | the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate | Sulfurisphaera tokodaii DSM 16993 | diphosphate + UDP-alpha-D-glucose | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
Sulfurisphaera tokodaii | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate | Sulfurisphaera tokodaii | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
r | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
Sulfurisphaera tokodaii DSM 16993 | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate | Sulfurisphaera tokodaii DSM 16993 | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
r | |
2.7.7.24 | diphosphate + dTDP-alpha-D-glucose | - |
Sulfurisphaera tokodaii | dTTP + alpha-D-glucose 1-phosphate | - |
r | |
2.7.7.24 | dTTP + alpha-D-glucose 1-phosphate | - |
Sulfurisphaera tokodaii | diphosphate + dTDP-alpha-D-glucose | - |
r | |
2.7.7.24 | dTTP + alpha-D-glucose 1-phosphate | the enzyme is involved in biosynthesis of L-rhamnose | Sulfurisphaera tokodaii | diphosphate + dTDP-alpha-D-glucose | - |
? | |
2.7.7.24 | dTTP + alpha-D-glucose 1-phosphate | - |
Sulfurisphaera tokodaii DSM 16993 | diphosphate + dTDP-alpha-D-glucose | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.B18 | ST0452 | - |
Sulfurisphaera tokodaii |
2.7.7.B19 | ST0452 | - |
Sulfurisphaera tokodaii |
2.7.7.B20 | ST0452 | - |
Sulfurisphaera tokodaii |
2.7.7.23 | N-acetyl-D-glucosamine-1-phosphate uridylyltransferase | - |
Sulfurisphaera tokodaii |
2.7.7.23 | ST0452 | - |
Sulfurisphaera tokodaii |
2.7.7.24 | glucose-1-phosphate thymidylyltransferase | - |
Sulfurisphaera tokodaii |
2.7.7.24 | ST0452 | - |
Sulfurisphaera tokodaii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.B18 | 95 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.B19 | 95 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.B20 | 95 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.23 | 95 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.24 | 95 | - |
- |
Sulfurisphaera tokodaii |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.B18 | 70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.B19 | 70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.B20 | 70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.23 | 70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.24 | 70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.B18 | 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
2.7.7.B18 | 95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
2.7.7.B19 | 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
2.7.7.B19 | 95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
2.7.7.B20 | 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
2.7.7.B20 | 95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
2.7.7.23 | additional information | - |
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C | Sulfurisphaera tokodaii |
2.7.7.23 | 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
2.7.7.23 | 95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
2.7.7.24 | 80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
2.7.7.24 | 95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.B18 | 8.5 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.B19 | 8.5 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.B20 | 8.5 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.23 | 8.5 | - |
- |
Sulfurisphaera tokodaii |
2.7.7.24 | 8.5 | - |
- |
Sulfurisphaera tokodaii |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.B18 | 6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.B19 | 6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.B20 | 6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.23 | 6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |
2.7.7.24 | 6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |