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Literature summary extracted from

  • MacLachlan, J.; Wotherspoon, A.T.L.; Ansell, R.O.; Brooks, C.J.W.
    Cholesterol oxidase: sources, physical properties and analytical applications (2000), J. Steroid Biochem. Mol. Biol., 72, 169-195.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Prescottella equi
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces violascens
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Schizophyllum commune
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Nocardia rhodochrous
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Pimelobacter simplex
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Nocardia erythropolis
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Brevibacterium sterolicum
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces griseocarneus
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Corynebacterium cholesterolicum
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Pseudomonas sp.
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces lavendulae
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Nocardia sp.
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Mycobacterium sp.
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces sp.
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces hygroscopicus
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Rhodococcus erythropolis
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Rhodococcus sp. (in: high G+C Gram-positive bacteria)
1.1.3.6 medicine determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments Streptomyces lividans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.6 expression in Streptomyces lividans Brevibacterium sterolicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.6 fenpropimorph irreversible inhibition; morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition Comamonas testosteroni
1.1.3.6 fenpropimorph morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive Nocardia erythropolis
1.1.3.6 fenpropimorph morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive Schizophyllum commune
1.1.3.6 fenpropimorph morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible competitive mechanism Streptomyces sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.6 60000
-
 x * 60000, SDS-PAGE Prescottella equi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.6 cholesterol + O2 Pseudomonas sp.
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Pimelobacter simplex
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Mycobacterium sp.
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Nocardia sp.
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Rhodococcus erythropolis
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces sp.
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Nocardia rhodochrous
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Nocardia erythropolis
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces lividans
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Schizophyllum commune
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces hygroscopicus
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces griseocarneus
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Prescottella equi
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces violascens
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Brevibacterium sterolicum
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Corynebacterium cholesterolicum
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Streptomyces lavendulae
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Rhodococcus sp. (in: high G+C Gram-positive bacteria)
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Comamonas testosteroni
-
 cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2 Rhodococcus sp. (in: high G+C Gram-positive bacteria) GK1
-
 cholest-5-en-3-one + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Brevibacterium sterolicum
-
-
-
1.1.3.6 Comamonas testosteroni
-
-
-
1.1.3.6 Corynebacterium cholesterolicum
-
-
-
1.1.3.6 Mycobacterium sp.
-
-
-
1.1.3.6 Nocardia erythropolis
-
-
-
1.1.3.6 Nocardia rhodochrous
-
-
-
1.1.3.6 Nocardia sp.
-
-
-
1.1.3.6 Pimelobacter simplex
-
-
-
1.1.3.6 Prescottella equi
-
-
-
1.1.3.6 Pseudomonas sp.
-
-
-
1.1.3.6 Rhodococcus erythropolis
-
-
-
1.1.3.6 Rhodococcus sp. (in: high G+C Gram-positive bacteria)
-
 solated from soil
-
1.1.3.6 Rhodococcus sp. (in: high G+C Gram-positive bacteria) GK1
-
 solated from soil
-
1.1.3.6 Schizophyllum commune
-
-
-
1.1.3.6 Streptomyces griseocarneus
-
-
-
1.1.3.6 Streptomyces hygroscopicus
-
-
-
1.1.3.6 Streptomyces lavendulae
-
-
-
1.1.3.6 Streptomyces lividans
-
-
-
1.1.3.6 Streptomyces sp.
-
-
-
1.1.3.6 Streptomyces violascens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.6 ammonium sulfate, ion-exchange chromatography, gel filtration Prescottella equi
1.1.3.6 choleterylglycine-CM-cellulose Pseudomonas sp.
1.1.3.6 DEAE-cellulose, cholesterol affinity column, Sephadex G-150 Pseudomonas sp.
1.1.3.6 partially purified by precipitation with ammonium sulfate Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.6 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 Prescottella equi
a
1.1.3.6 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 Streptomyces violascens
a
1.1.3.6 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 Schizophyllum commune
a
1.1.3.6 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
a
1.1.3.6 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 Pimelobacter simplex
a
1.1.3.6 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
a
1.1.3.6 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 Brevibacterium sterolicum
a
1.1.3.6 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 Streptomyces griseocarneus
a
1.1.3.6 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
a
1.1.3.6 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 Pseudomonas sp.
a
1.1.3.6 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 Streptomyces lavendulae
a
1.1.3.6 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 sp.
a
1.1.3.6 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 Mycobacterium sp.
a
1.1.3.6 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 Streptomyces sp.
a
1.1.3.6 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 Streptomyces hygroscopicus
a
1.1.3.6 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 erythropolis
a
1.1.3.6 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. (in: high G+C Gram-positive bacteria)
a
1.1.3.6 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 Streptomyces lividans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Pseudomonas sp. cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Pimelobacter simplex cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Mycobacterium sp. cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia sp. cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus erythropolis cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces sp. cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia rhodochrous cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia erythropolis cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces lividans cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Schizophyllum commune cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces hygroscopicus cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces griseocarneus cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Prescottella equi cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces violascens cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Brevibacterium sterolicum cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Corynebacterium cholesterolicum cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces lavendulae cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus sp. (in: high G+C Gram-positive bacteria) cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Comamonas testosteroni cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus sp. (in: high G+C Gram-positive bacteria) GK1 cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Pseudomonas sp. cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Pimelobacter simplex cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Mycobacterium sp. cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia sp. cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus erythropolis cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces sp. cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia rhodochrous cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Nocardia erythropolis cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces lividans cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Schizophyllum commune cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces hygroscopicus cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces griseocarneus cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Prescottella equi cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces violascens cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Brevibacterium sterolicum cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Corynebacterium cholesterolicum cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Streptomyces lavendulae cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus sp. (in: high G+C Gram-positive bacteria) cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Comamonas testosteroni cholest-5-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus sp. (in: high G+C Gram-positive bacteria) GK1 cholest-5-en-3-one + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.6 ? x * 60000, SDS-PAGE Prescottella equi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.6 6 8.2 membrane bound enzyme Rhodococcus sp. (in: high G+C Gram-positive bacteria)
1.1.3.6 7 7.5 extracellular enzyme Rhodococcus sp. (in: high G+C Gram-positive bacteria)