EC Number   |
Protein Variants |
Reference  |
|---|
    1.8.2.1 | G473A |
mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type |
667714 |
| 1.8.2.1 | G473D |
monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation |
667714 |
| 1.8.2.1 | G473W |
monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation |
667714 |
| 1.8.2.1 | R212A/G473D |
mutant is able to oligomerize but has undetectable activity, significant random-coil formation |
667714 |
| 1.8.2.1 | Y236F |
reduced turnover rates and substrate affinity as well as an altered reactivity toward molecular oxygen as an electron acceptor, unlike the wild type enzyme the mutant enzyme is reoxidized quickly in the presence of molecular oxygen |
667744 |
| 1.8.2.1 | Y236F |
near Mo center |
700633 |
| 1.8.2.1 | P105A |
the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme |
711223 |
| 1.8.2.1 | P105A/P111A |
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme |
711223 |
| 1.8.2.1 | P111A |
the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme |
711223 |
| 1.8.2.1 | C185A |
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor |
711242 |
