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Literature summary extracted from

  • Pollegioni, L.; Gadda, G.; Ambrosius, D.; Ghisla, S.; Pilone, M.S.
    Cholesterol oxidase from Streptomyces hycroscopicus and Brevibacterium sterolicum: effect of surfactants and organic solvents on activity (1999), Biotechnol. Appl. Biochem., 30, 27-33.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.3.6 dodecylpoly(ethylene glycol ether)9-10 trivial name thesit, 0.1 mM cholesterol: increase in enzyme activity in the presence of 0.1% to 2% thesit, 0.34 mM cholesterol: sharp decrease with increasing thesit concentrations Streptomyces hygroscopicus
1.1.3.6 dodecylpoly(ethylene glycol ether)9-10 trivial name thesit, 0.1 mM cholesterol: increase in enzyme activity in the presence of 0.1% to 2% thesit, 0.34 mM cholesterol: sharp decrease with increasing thesit concentrations Brevibacterium sterolicum
1.1.3.6 phosphate ions marked increase above 90 mM Streptomyces hygroscopicus
1.1.3.6 phosphate ions marked increase above 90 mM Brevibacterium sterolicum
1.1.3.6 propan-2-ol maximal enzyme activity with 10%(v/v) in the presence of 500 mM potassium phosphate, decrease in activity in the presence of 50 mM potassium phosphate Streptomyces hygroscopicus

General Stability

EC Number General Stability Organism
1.1.3.6 65% activity remains after 24 h at 25°C in 50 mM potassium phosphate, pH 7.5, enzyme is completely stable for 300 min in the presence of 1% propan-2-ol and 1% thesit as well as in the presence of 10% propan-2-ol and 8% thesit Streptomyces hygroscopicus
1.1.3.6 65% activity remains after 24 h at 25°C in 50 mM potassium phosphate, pH 7.5, enzyme is completely stable for 300 min in the presence of 1% propan-2-ol and 1% thesit as well as in the presence of 10% propan-2-ol and 8% thesit Brevibacterium sterolicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.6 Triton X-100 strong decrease in enzyme activity at concentration of 0.2% Triton X-100 or higher Brevibacterium sterolicum
1.1.3.6 Triton X-100 strong decrease in enzyme activity at concentration of 0.2% Triton X-100 or higher Streptomyces hygroscopicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.6 0.4
-
dehydroepiandrosterone
-
Brevibacterium sterolicum

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 Streptomyces hygroscopicus
-
cholest-5-en-3-one + H2O2
-
?
1.1.3.6 cholesterol + O2 Brevibacterium sterolicum
-
cholest-5-en-3-one + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Brevibacterium sterolicum
-
-
-
1.1.3.6 Streptomyces hygroscopicus
-
-
-

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 Streptomyces hygroscopicus
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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
Streptomyces hygroscopicus 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
-
Streptomyces hygroscopicus cholest-5-en-3-one + H2O2
-
?
1.1.3.6 cholesterol + O2
-
Brevibacterium sterolicum cholest-5-en-3-one + H2O2
-
?