EC Number   |
Protein Variants |
Reference |
|---|
   7.3.2.7 | C108A |
alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain |
719496 |
| 7.3.2.7 | C113A/C422A |
mutant ArsA has basal ATPase activity similar to that of the wild type but lacks metalloid-stimulated activity |
-, 669530 |
| 7.3.2.7 | C113A/C422A |
site-directed mutagenesis, the mutant lacks As(III) activation activity compared to the wild-type enzyme |
689052 |
| 7.3.2.7 | C120A |
alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain |
719496 |
| 7.3.2.7 | C172A |
site-directed mutagenesis, an ArsA mutant, the mutant shows reduced affinity for Sb(III) compared to the wild-type enzyme |
689052 |
| 7.3.2.7 | C172A/H453A |
site-directed mutagenesis, the ArsA double mutant exhibits significantly decreased affinity for Sb(III) |
689052 |
| 7.3.2.7 | D137V |
inactive |
733473 |
| 7.3.2.7 | D142A |
site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme |
696278 |
| 7.3.2.7 | D142E |
site-directed mutagenesis, the mutant is stronger activated by arsenite and antimonite compared to the wild-type enzyme |
696278 |
| 7.3.2.7 | D142N |
site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme |
696278 |
