Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.6 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
Search for more literature for 1.1.3.6

Activating Compound

Activating Compound Comment Organism Structure
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
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
phosphate ions marked increase above 90 mM Streptomyces hygroscopicus
phosphate ions marked increase above 90 mM Brevibacterium sterolicum
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

General Stability Organism
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
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

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cholesterol + O2 Streptomyces hygroscopicus
-
 cholest-5-en-3-one + H2O2
-
 ?
cholesterol + O2 Brevibacterium sterolicum
-
 cholest-5-en-3-one + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
-
-
-
Streptomyces hygroscopicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
 Streptomyces hygroscopicus cholest-4-en-3-one + H2O2
-
 ?
cholesterol + O2
-
 Brevibacterium sterolicum cholest-4-en-3-one + H2O2
-
 ?
cholesterol + O2
-
 Streptomyces hygroscopicus cholest-5-en-3-one + H2O2
-
 ?
cholesterol + O2
-
 Brevibacterium sterolicum cholest-5-en-3-one + H2O2
-
 ?