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Literature summary for 1.1.3.6 extracted from

  • Bru, R.; Sanchez-Ferrer, A.; Garcia-Carmona, F.
    Characterization of cholesterol oxidase activity in AOT-isooctane reverse micelles and its dependence on micelle size (1989), Biotechnol. Lett., 11, 237-242.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
cholesterol Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane Nocardia erythropolis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Nocardia erythropolis
-
-
-

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 Nocardia erythropolis

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Nocardia erythropolis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + O2
-
Nocardia erythropolis cholest-4-en-3-one + H2O2
-
?
cholesterol + O2
-
Nocardia erythropolis cholest-5-en-3-one + H2O2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
enzyme after micellization Nocardia erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
enzyme after micellization Nocardia erythropolis