EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.6 | cholesterol + O2 | Bordetella sp. | - |
cholest-4-en-3-one + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.6 | Bordetella sp. | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.6 | cholesterol + O2 | - |
Bordetella sp. | cholest-4-en-3-one + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.3.6 | COD | - |
Bordetella sp. |
1.1.3.6 | COD-B | - |
Bordetella sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.6 | FAD | - |
Bordetella sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.3.6 | physiological function | cholesterol oxidase from Bordetella species promotes irreversible cell apoptosis in lung adenocarcinoma by cholesterol oxidation in vitro and in vivo. COD-B treatment results in JNK and p38 phosphorylation, downregulation of Bcl-2, upregulation of Bax, activated caspase-3 and cytochrome C release, which likely responds to freshly produced hydrogen peroxide that accompanies cholesterol oxidation. COD-B leads to irreversible cell apoptosis by decreasing cholesterol content and increasing reactive oxygen species level. Cholesterol oxidase (COD) is a flavoprotein that catalyzes the oxidation of cholesterol to 4-cholesten-3-one with the reduction of oxygen to hydrogen peroxide. COD can convert membrane cholesterol to 4-cholesten-3-one and can inhibit the formation of lipid rafts. Different from other cholesterol-depleting agents, COD disrupts lipid rafts by displacing cholesterol with 4-cholesten-3-one. COD-B catalyzes the oxidation of membrane cholesterol in lung adenocarcinoma cell. When cells are pretreated with catalase before adding COD-B and cholesterol, the phosphorylation of Akt and ERK1/2 remaines attenuated compared with the group without catalase treatment. Catalase pretreatment also partially blocks the activation of caspase-3, effect of catalase on the COD-B-induced signaling response, overview. COD-B induces the reversible translocation of caveolin-1, which is involved in trafficking membrane cholesterol, in a cholesterol-reversable manner | Bordetella sp. |