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Literature summary for 1.1.3.6 extracted from

  • Cheillan, F.; Lafont, H.; Termine, E.; Fernandez, F.; Sauve, P.; Lesgards, G.
    Molecular characteristics of the cholesterol oxidase and factors influencing its activity (1989), Biochim. Biophys. Acta, 999, 233-238.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
Bile salts
-
Pseudomonas sp.

General Stability

General Stability Organism
bile salts stabilize Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
cholesterol
-
Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65100
-
analytical ultracentrifugation Pseudomonas sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

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 Pseudomonas sp.

Substrates and Products (Substrate)

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