EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.4.2.8 | structure in the unliganded form, in complex with IMP and in complex with GMP, to 2.1, 1.9 and 2.2 A resolution, respectively. The overall fold of the IMP complex is similar to that of the unliganded form, but the main-chain and side-chain atoms of the active site move to accommodate IMP. The overall folds of the IMP and GMP complexes are almost identical to each other. Enzyme belongs to group I | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.2.8 | 0.0039 | - |
hypoxanthine | pH 7.9, 25°C | Thermus thermophilus | |
2.4.2.8 | 0.0074 | - |
guanine | pH 7.9, 25°C | Thermus thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.2.8 | Thermus thermophilus | Q5SLS3 | - |
- |
2.4.2.8 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SLS3 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.8 | guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | GMP + diphosphate | - |
? | |
2.4.2.8 | guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | GMP + diphosphate | - |
? | |
2.4.2.8 | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | IMP + diphosphate | - |
? | |
2.4.2.8 | hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | IMP + diphosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.2.8 | HGPRTase | - |
Thermus thermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.2.8 | 9.1 | - |
hypoxanthine | pH 7.9, 25°C | Thermus thermophilus | |
2.4.2.8 | 20 | - |
guanine | pH 7.9, 25°C | Thermus thermophilus |