EC Number   |
Protein Variants |
Reference |
|---|
    3.5.4.2 | C127A |
10fold decrease in kcat over the wild-type |
-, 755347 |
| 3.5.4.2 | C127S |
complete loss of activity |
-, 755347 |
| 3.5.4.2 | D118N |
mutant is able to bind 2 metals per active site, kcat (adenine): 173/sec |
718893 |
| 3.5.4.2 | D284A |
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction |
718893 |
| 3.5.4.2 | D285A |
mutant is able to bind 2 metals per active site, kcat (adenine): 37/sec |
718893 |
| 3.5.4.2 | D474N |
mutant is able to bind 2 metals per active site, kcat (adenine): 171/sec |
718893 |
| 3.5.4.2 | E121Q |
mutant is able to bind 2 metals per active site, kcat (adenine): 57/sec |
718893 |
| 3.5.4.2 | E185Q |
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site |
718893 |
| 3.5.4.2 | E236Q |
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction |
718893 |
| 3.5.4.2 | H120N |
mutant is able to bind 2 metals per active site, kcat (adenine): 0.13/sec |
718893 |
