EC Number   |
Protein Variants |
Reference |
|---|
   1.3.3.5 | biotechnology |
bilirubin oxidase has been found to be the best enzyme for converting O2 to H2O as a cathodic enzyme in biofuel cells |
686068 |
| 1.3.3.5 | C457A |
no oxidase activity |
391035 |
| 1.3.3.5 | C457S |
can react with dioxygen, affords reaction intermediate I with absorption maxima at 340, 470, and 675 nm |
672031 |
| 1.3.3.5 | C457S |
virtually no enzyme activity, Ru-incorporation conferrs higher enzyme activity |
673257 |
| 1.3.3.5 | C457V |
no oxidase activity |
391035 |
| 1.3.3.5 | D105A |
exhibits 7.5% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II |
672031 |
| 1.3.3.5 | D105E |
exhibits 46% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II |
672031 |
| 1.3.3.5 | D105N |
does not react with dioxygen |
672031 |
| 1.3.3.5 | E463Q |
site-directed mutagenesis |
712025 |
| 1.3.3.5 | H134/136V |
no oxidase activity |
391035 |
