IntEnz

EC 1.1.3.6 - Cholesterol oxidase

IntEnz Enzyme Nomenclature
EC 1.1.3.6

Names

Reaction

• 32183 [IUBMB]
  cholesterol

  cholesterol

  Name origin: UniProt - CHECKED (C)

  CHEBI:16113

  Formula: C27H46O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  O₂

  O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:15379

  Formula: O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  cholest-5-en-3-one

  cholest-5-en-3-one

  Name origin: UniProt - CHECKED (C)

  CHEBI:63906

  Formula: C27H44O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O₂

  H2O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16240

  Formula: H2O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

Cofactor

• FAD

Comments:

Contains flavin adenine dinucleotide (FAD). Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ⁵ position to the Δ⁶ position (cf. EC 5.3.3.1, steroid Δ-isomerase).

Links to other databases

References

1. Richmond, W.
   Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum.
   Clin. Chem. 19: 1350-1356 (1973). [PMID: 4757363]
2. Stadtman, T.C., Cherkes, A. and Anfinsen, C.B.
   Studies on the microbiological degradation of cholesterol.
   J. Biol. Chem. 206: 511-523 (1954). [PMID: 13143010]
3. MacLachlan, J., Wotherspoon, A. T., Ansell, R. O., Brooks, C. J.
   Cholesterol oxidase: sources, physical properties and analytical applications.
   J. Steroid Biochem. Mol. Biol. 72: 169-195 (2000). [PMID: 10822008]
4. Vrielink, A.
   Cholesterol oxidase: structure and function.
   Subcell. Biochem. 51: 137-158 (2010). [PMID: 20213543]

[EC 1.1.3.6 created 1961, modified 1982, modified 2012]