EC Number |
Protein Variants |
Reference |
---|
1.8.2.1 | C185A |
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor |
711242 |
1.8.2.1 | C185S |
the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor |
711242 |
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 | H57A |
heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent |
724418 |
1.8.2.1 | H57A |
mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate |
722663 |
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 |