|
In enzymology, a cholesterol oxidase () is an enzyme that catalyzes the chemical reaction :cholesterol + O2 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. ==Structural studies== As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Cholesterol oxidase」の詳細全文を読む スポンサード リンク
|