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Literature summary extracted from

  • Johnson, T.L.; Somkuti, G.A.
    Isolation of cholesterol oxidases from Rhodococcus equi ATCC 33706 (1991), Biotechnol. Appl. Biochem., 13, 196-204.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.6 cholesterol + O2 Rhodococcus equi
-
 cholest-5-en-3-one + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Rhodococcus equi
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.6 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 Rhodococcus equi
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Rhodococcus equi cholest-4-en-3-one + H2O2
-
 ?
1.1.3.6 cholesterol + O2
-
 Rhodococcus equi cholest-5-en-3-one + H2O2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.6 40
-
-
 Rhodococcus equi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.6 6 8 extracellular enzyme Rhodococcus equi
1.1.3.6 8
-
 membrane-bound enzyme Rhodococcus equi