EC Number |
Protein Variants |
Reference |
---|
7.2.1.3 | D38A |
the mutant shows increased Fe(CN)3 reductase activity compared to the wild type enzyme |
673552 |
7.2.1.3 | D38A |
the mutation of lysosomal cytochrome b561 increases the enzyme activity compared to the wild type |
756694 |
7.2.1.3 | E117A |
the mutant shows decreased Fe(CN)3 reductase activity compared to the wild type enzyme |
673552 |
7.2.1.3 | E177A |
the mutation of lysosomal cytochrome b561 reduces the enzyme activity compared to the wild type |
756694 |
7.2.1.3 | E196A |
the mutant shows decreased Fe(CN)3 reductase activity compared to the wild type enzyme |
673552 |
7.2.1.3 | E196A |
the mutation of lysosomal cytochrome b561 strongly reduces the enzyme activity compared to the wild type |
756694 |
7.2.1.3 | E79A |
site-directed mutagenesis, the mutation in bovine rCGCytb causes significant (but no extreme) alteration in at least one of the two (sometimes three) midpoint ascorbate concentrations characterizing the redox transition of hemes-b, and the mutation does not block the reduction of either heme-b center |
744757 |
7.2.1.3 | F105W/H106E |
mutations on the noncytoplasmic side only still allows the oxidized Cyt b561 to be reduced by ascorbate |
728698 |
7.2.1.3 | F184A |
35% residual activity |
750349 |
7.2.1.3 | F44A |
the mutation of lysosomal cytochrome b561 reduces the enzyme activity by about 45% compared to the wild type |
756694 |