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Literature summary for 1.1.3.6 extracted from

  • Uwajima, T.; Terada, O.
    On the kinetics of cholesterol oxidase from Brevibacterium sterolicum in the presence of detergents (1978), Agric. Biol. Chem., 42, 1453-1454.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
cholic acid stimulates without a significant change in Km in the presence of low Triton X-100 concentrations, changes the sigmoidal kinetic into normal Michaelis-Menten kinetic with reduced Km in the presence of high Triton X-100 concentrations Brevibacterium sterolicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32500
-
gel filtration, sedimentation equilibrium Brevibacterium sterolicum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
-
-
-

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 Brevibacterium sterolicum

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Brevibacterium sterolicum

Cofactor

Cofactor Comment Organism Structure
FAD firmly bound Brevibacterium sterolicum
FAD flavoprotein Brevibacterium sterolicum