Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.6 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)

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

Organism

Organism UniProt Comment Textmining
Rhodococcus equi
-
-
-

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 Rhodococcus equi

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

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