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Literature summary for 2.7.4.9 extracted from
- Structural and functional roles of dynamically correlated residues in thymidylate kinase (2018), Acta Crystallogr. Sect. D, 74, 341-354 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| high-resolution X-ray crystal structures of thymidylate kinase in apo and ligand-bound states, structures of binary and ternary complexes of thymidylate kinase with its natural substrates ATP and ATP-TMP, respectively | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D90L | high similarity to the wild-type. Less than 10% of wild-type activity | Thermus thermophilus |
| K16M | high similarity to the wild-type. Less than 10% of wild-type activity | Thermus thermophilus |
| T18V | equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure. Increase in thermal stability by 3.4°C | Thermus thermophilus |
| V158T | equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure, thermal stability similar to that of wild-type enzyme | Thermus thermophilus |
| Y162F | equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure | Thermus thermophilus |
| Y162F | significant decrease in thermal stability of 10 °C as compared with wild-type enzyme | Thermus thermophilus |
| Y92H | equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure, significant decrease in thermal stability of 8.8 °C as compared with wild-type enzyme | Thermus thermophilus |
| Y99F | high similarity to the wild-type, activity is about 60% of the wild-type activity | Thermus thermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Thermus thermophilus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + dTMP | Thermus thermophilus | - |
ADP + dTDP | - |
? | |
| ATP + dTMP | Thermus thermophilus ATCC 27634 | - |
ADP + dTDP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q5SHX3 | - |
- |
| Thermus thermophilus ATCC 27634 | Q5SHX3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + dTMP | - |
Thermus thermophilus | ADP + dTDP | - |
? | |
| ATP + dTMP | - |
Thermus thermophilus ATCC 27634 | ADP + dTDP | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 89.2 | - |
Tm-value of wild-type enzyme | Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | important enzyme in DNA synthesis | Thermus thermophilus |
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Release 2023.1 (January 2023)
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