Cholesterol Binding and Cholesterol Transport Proteins:

Volume 51 of the series Subcellular Biochemistry pp 137-158


Cholesterol Oxidase: Structure and Function

  • Alice VrielinkAffiliated withSchool of Biomedical Biomolecular and Chemical Sciences, University of Western Australia Email author 

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Cholesterol oxidase is a bacterial-specific flavoenzyme that catalyzes the oxidation and isomerisation of steroids containing a 3β hydroxyl group and a double bond at the Δ5–6 of the steroid ring system. The enzyme is a member of a large family of flavin-specific oxidoreductases and is found in two different forms: one where the flavin adenine dinucleotide (FAD) cofactor is covalently linked to the protein and one where the cofactor is non-covalently bound to the protein. These two enzyme forms have been extensively studied in order to gain insight into the mechanism of flavin-mediated oxidation and the relationship between protein structure and enzyme redox potential. More recently the enzyme has been found to play an important role in bacterial pathogenesis and hence further studies are focused on its potential use for future development of novel antibacterial therapeutic agents. In this review the biochemical, structural, kinetic and mechanistic features of the enzyme are discussed.


Cholesterol oxidase Flavoenzyme Enzyme mechanism Redox catalysis Oxygen channel Protein structure