EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.17 | G230S |
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme |
-, 736541 |
| 2.4.2.17 | K50A |
2.3fold increase in kcat, 51fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.8fold increase in Km-value for ATP |
678174 |
| 2.4.2.17 | K8A |
2.5fold decrease in kcat, 4.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 3.1fold increase in Km-value for ATP |
678174 |
| 2.4.2.17 | L231F/T235A |
conserved residues |
721765 |
| 2.4.2.17 | more |
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit |
-, 736541 |
| 2.4.2.17 | N215K |
conserved residue |
721765 |
| 2.4.2.17 | N215K/L231F/T235A |
conserved residues, 37fold increase in Ki-value of histidine |
721765 |
| 2.4.2.17 | N215K/L231F/T235A/A270P |
conserved residues |
721765 |
| 2.4.2.17 | R216A |
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability |
-, 758921 |
| 2.4.2.17 | R216Q |
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine |
-, 758921 |
