Cholesterol oxidase: biotechnological applications

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Pollegioni L, Piubelli L, Molla G

Cholesterol oxidase: biotechnological applications

The Febs Journal. 2009 Nov 16;276(23):6857-6870.

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Abstract

Cholesterol oxidase is a bacterial FAD‐containing flavooxidase that catalyzes the first reaction in cholesterol catabolism. Indeed, this enzyme catalyzes two reactions: the oxidation of the C3‐OH group of cholesterol (and other sterols) to give cholest‐5‐en‐3‐one; and its isomerization to cholest‐4‐en‐3‐one. In the past several years, the structural and functional characterization of cholesterol oxidase has been developed together with its application as a biological tool. Cholesterol oxidase has been used in biocatalysis for the production of a number of steroids, as an insecticidal protein against boll weevil larvae and, in particular, as a diagnostic enzyme for determining serum levels of cholesterol. These applications prompted various laboratories worldwide to isolate this flavooxidase from different sources and to improve its properties by protein engineering, further increasing our knowledge on its structure–function relationships. These studies also discovered new physiological roles for cholesterol oxidase (e.g. in virulence and as an antifungal sensor). We assume that the investigations of cholesterol oxidase and its applications will continue to grow quickly in the near future, in particular to uncover unexpected, new areas of application.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Prasterone	Cholesterol oxidase	Protein	Brevibacterium sterolicum	Unknown	Substrate	Details