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Review
. 2017 Feb 1;364(3).
doi: 10.1093/femsle/fnx007.

Microbial catabolism of sterols: focus on the enzymes that transform the sterol 3β-hydroxy-5-en into 3-keto-4-en

Review

Microbial catabolism of sterols: focus on the enzymes that transform the sterol 3β-hydroxy-5-en into 3-keto-4-en

Joseph Kreit. FEMS Microbiol Lett. .

Abstract

An overview on the microbial sterol catabolism is described with a focus on the catabolic step of the 3β-hydroxy-5-en structure. Cholesterol oxidase transforms this structure into the corresponding 3-keto-4-en feature, and thus initiates the sterol molecule catabolism. The oxidase has been found in a large number of microorganisms, especially in Actinobacteria as species of Rhodococcus and Streptomyces. Other Actinobacteria as species of Mycobacterium and Nocardia possess NAD(P)-dependent dehydrogenase for this catabolic step. In Rhodococcus jostii, oxidation of the C26 of the sterol side chain is the initiating step. The resulting stenone or sterol-C26-oic acid is then catabolized according to two subpathways: cleavage of the sterol side chain and degradation of the steroid nucleus. Divergent items concerned with the enzymes that transform the sterol 3β-hydroxy-5-en are discussed.

Keywords: 3β-hydroxysteroid dehydrogenase; Mycobacterium; Nocardia; Rhodococcus; cholesterol oxidase; sterol catabolism.

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