1.1.3.6 3beta-chlorocholest-5-ene + O2 low activity 1.1.3.6 androst-4-ene-3,17-dione + O2 - 1.1.3.6 beta-cholestanol + O2 101% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 13% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 69% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 75% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 78% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 79% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 95% activity compared to cholesterol 1.1.3.6 beta-cholestanol + O2 96% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 20% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 29% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 39% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 50% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 64% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 72% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 80% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 84% activity compared to cholesterol 1.1.3.6 beta-sitosterol + O2 - 1.1.3.6 beta-stigmasterol + O2 10% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 12% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 17% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 32% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 36% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 37% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 40% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 47% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 50% activity compared to cholesterol 1.1.3.6 beta-stigmasterol + O2 59% activity compared to cholesterol 1.1.3.6 cholest-4-en-3-one + O2 - 1.1.3.6 cholesterol + O2 - 1.1.3.6 cholesterol + O2 100% activity 1.1.3.6 cholesterol + O2 cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin 1.1.3.6 cholesterol + O2 cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor 1.1.3.6 cholesterol + O2 via cholest-5-en-3-one 1.1.3.6 cholesterol + O2 first step in cholesterol degradation 1.1.3.6 dehydroandrosterone + O2 - 1.1.3.6 dehydroepiandrosterone + O2 16% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 24% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 27% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 28% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 37% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 41% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 48% activity compared to cholesterol 1.1.3.6 dehydroepiandrosterone + O2 5% activity compared to cholesterol 1.1.3.6 diosgenin + O2 - 1.1.3.6 epiandrosterone + O2 1% activity compared to cholesterol 1.1.3.6 epiandrosterone + O2 10% activity compared to cholesterol 1.1.3.6 epiandrosterone + O2 15% activity compared to cholesterol 1.1.3.6 ergosterol + O2 12% activity compared to cholesterol 1.1.3.6 ergosterol + O2 14% activity compared to cholesterol 1.1.3.6 ergosterol + O2 17% activity compared to cholesterol 1.1.3.6 ergosterol + O2 20% activity compared to cholesterol 1.1.3.6 ergosterol + O2 4% activity compared to cholesterol 1.1.3.6 ergosterol + O2 5% activity compared to cholesterol 1.1.3.6 ergosterol + O2 51% activity compared to cholesterol 1.1.3.6 additional information no activity with dehydroepiandrosterone 1.1.3.6 additional information cholesterol oxidase is involved in pimaricin biosynthesis 1.1.3.6 additional information intact ChoD is important for the growth of Mycobacterium tuberculosis in peritoneal macrophages and lungs of mice. Cholesterol oxidase is required for virulence of Mycobacterium tuberculosis 1.1.3.6 additional information no activity with ergosterol 1.1.3.6 additional information no activity with ergosterol, pregnenolone, dehydroepiandrosterone, and epiandosterone 1.1.3.6 additional information the oxidation of the allylic alcohols by cholesterol oxidase from Rhodococcus erythropolis is stereo- and enantioselective. The enzyme oxidizes (S)-alcohol at a higher rate than (R)-alcohol 1.1.3.6 additional information cholesterol oxidase is a bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one while dioxygen is finally reduced to H2O2 as by-product. The enzymatic overall cholesterol oxidation comprises three steps. In the first one the 3beta-OH group of cholesterol is oxidized to the corresponding ketone with the concomitant reduction of the FAD cofactor. In a second step an isomerization of the double bond from the DELTA5-6 position to the DELTA4-5 position takes place. The FAD is recycled in a redox reaction with dioxygen, yielding hydrogen peroxide 1.1.3.6 additional information cholesterol oxidase is a bifunctional FAD-containing oxidoreductase which catalyzes the oxidation and isomerization of cholesterol into 4-cholesten-3-one 1.1.3.6 additional information cholesterol oxidase is a bifunctional flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one 1.1.3.6 pregnenolone + O2 20% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 22% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 32% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 37% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 38% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 42% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 6% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 95% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 99% activity compared to cholesterol 1.1.3.6 pregnenolone + O2 -