Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells | Sulfurisphaera tokodaii |
Protein Variants | Comment | Organism |
---|---|---|
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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
dTTP | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
0.05 | - |
dTDP-alpha-D-glucose | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
0.39 | - |
diphosphate | pH 8.0, 80°C | Sulfurisphaera tokodaii | |
1.12 | - |
alpha-D-glucose 1-phosphate | pH 8.0, 80°C | Sulfurisphaera tokodaii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | |
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 | |
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 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dTTP + alpha-D-glucose 1-phosphate | Sulfurisphaera tokodaii | the enzyme is involved in biosynthesis of L-rhamnose | diphosphate + dTDP-alpha-D-glucose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfurisphaera tokodaii | Q975F9 | - |
- |
Sulfurisphaera tokodaii DSM 16993 | Q975F9 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Sulfurisphaera tokodaii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
diphosphate + dTDP-alpha-D-glucose | - |
Sulfurisphaera tokodaii | dTTP + alpha-D-glucose 1-phosphate | - |
r | |
dTTP + alpha-D-glucose 1-phosphate | - |
Sulfurisphaera tokodaii | diphosphate + dTDP-alpha-D-glucose | - |
r | |
dTTP + alpha-D-glucose 1-phosphate | the enzyme is involved in biosynthesis of L-rhamnose | Sulfurisphaera tokodaii | diphosphate + dTDP-alpha-D-glucose | - |
? | |
dTTP + alpha-D-glucose 1-phosphate | - |
Sulfurisphaera tokodaii DSM 16993 | diphosphate + dTDP-alpha-D-glucose | - |
r |
Synonyms | Comment | Organism |
---|---|---|
glucose-1-phosphate thymidylyltransferase | - |
Sulfurisphaera tokodaii |
ST0452 | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
95 | - |
- |
Sulfurisphaera tokodaii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | 100 | 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity | Sulfurisphaera tokodaii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
half-life: 180 min | Sulfurisphaera tokodaii |
95 | - |
half-life: 60 min | Sulfurisphaera tokodaii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
- |
Sulfurisphaera tokodaii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 10 | pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity | Sulfurisphaera tokodaii |