EC Number   |
General Information |
Reference |
|---|
   1.3.3.5 | evolution |
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions |
724076 |
| 1.3.3.5 | evolution |
the enzyme belongs to the family of multicopper oxidases (MCOs) |
-, 745422 |
| 1.3.3.5 | evolution |
the enzyme belongs to the multicopper oxidase (MCO) family. These enzymes have four copper atoms that are classified into three types according to their spectroscopic and magnetic properties: type I (T1), type II (T2) and type III (T3) Cu. The MCO family can be separated into two types by substrate specificity. The first group catalyzes the outer sphere oxidation of small organic substrates and include the plant and fungal laccases and ascorbate oxidase, CotA, bilirubin oxidase, and phenoxazinone synthase |
746191 |
| 1.3.3.5 | evolution |
the enzyme is a CotA multicopper oxidase, MCO |
724607 |
| 1.3.3.5 | more |
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions |
724076 |
| 1.3.3.5 | more |
dissociation of type I copper, caused by thermal inactivation, is accompanied by a conformational change and a decrease in secondary structure |
710859 |
| 1.3.3.5 | physiological function |
bilirubin oxidase (BOD) is one of the multicopper oxidoreductases family with many interesting possible biotechnological applications, including biocatalytic reduction of oxygen (O2) at natural pH, biosensing, biobleaching, bioremediation, chemical synthesis, and wine stabilization |
744715 |
| 1.3.3.5 | physiological function |
the enzyme is a copper-containing oxidase that catalyzes oxidation of various organic compounds, including phenolic ones, by molecular oxygen, the latter is reduced to water via a fourelectron mechanism |
744280 |
