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Literature summary for 1.1.3.6 extracted from

  • Stadman, T.C.; Cherkes, A.; Anfinsen, C.B.
    Studies on the microbiological degradation of cholesterol (1953), J. Biol. Chem., 206, 511-523.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by 10 mM cyanide or 50 mM arsenite Mycobacterium sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mycobacterium sp.
-
probably identical with cholesterol decompositing Mycobacterium cholesterolicum
-

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 Mycobacterium sp.

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
50% loss of activity after 10 min Mycobacterium sp.

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 strong decrease in enzyme activity above Mycobacterium sp.