Cholesterol oxidase explained

cholesterol oxidase
Ec Number:1.1.3.6
Cas Number:9028-76-6
Go Code:0016995
Symbol:Chol_subst-bind
Cholesterol oxidase substrate-binding domain
Pfam:PF09129
Pfam Clan:CL0277
Interpro:IPR015213
Scop:1i19

In enzymology, a cholesterol oxidase is an enzyme that catalyzes the chemical reaction

cholesterol + O2

\rightleftharpoons

cholest-4-en-3-one + H2O2

Thus, the two substrates of this enzyme are cholesterol and O2, whereas its two products are cholest-4-en-3-one and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. Other names in common use include cholesterol- O2 oxidoreductase, 3beta-hydroxy steroid oxidoreductase, and 3beta-hydroxysteroid:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis.

The substrate-binding domain found in some bacterial cholesterol oxidases is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one.[1]

Structural studies

As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,,,,,, and .

Further reading

Notes and References

  1. Coulombe R, Yue KQ, Ghisla S, Vrielink A . Alice Vrielink. Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair . J. Biol. Chem. . 276 . 32 . 30435–41 . August 2001 . 11397813 . 10.1074/jbc.M104103200 . free .