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Information on EC 1.1.3.6 - cholesterol oxidase
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1.1.3.6 cholesterol oxidaseIUBMB Comments
Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta5 position to Delta6 position (cf. EC 5.3.3.1, steroid Delta-isomerase).
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Word Map
- 1.1.3.6
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biosensors
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electrode
- esterase
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electrochemical
- brevibacterium
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fabric
- oxidases
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amperometric
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film
- rhodococcus
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raft
- cholestenone
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voltammetry
- cholest-4-en-3-one
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flavoenzyme
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cholesteryl
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nanocomposite
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biosensing
- erythropolis
- filipin
- 4-cholesten-3-one
- nocardia
- medicine
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3hcholesterol
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electropolymerization
- lavendulae
- biotechnology
- agriculture
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co-immobilized
- methyl-beta-cyclodextrin
- diagnostics
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bioelectrode
- luminol
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screen-printed
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electrocatalytic
- analysis
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3.1.1.13
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polypyrrole
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multiwalled
- beta-ol
- synthesis
- drug development
The enzyme appears in viruses and cellular organisms
Synonyms
cholesterol oxidase, coase, chori, chom2, chorii, cholox, cho-u, chom1, cod-b, cholesterol oxidase ii, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
Nocardia rhodochrous
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
Nocardia erythropolis
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
Corynebacterium cholesterolicum
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
cholesterol + O2 = cholest-5-en-3-one + H2O2
isomerization is not the rate limiting step
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cholesterol + O2 = cholest-5-en-3-one + H2O2
isomerization is not the rate limiting step
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cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
Rhodococcus sp. GK1
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cholesterol + O2 = cholest-5-en-3-one + H2O2
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