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

AbstractAn 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 f...

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Bibliographic Details
Published in:FEMS microbiology letters 2017-02, Vol.364 (3)
Main Author: Kreit, Joseph
Format: Article
Language:English
Subjects:
Actinobacteria
Bacteriology
Biodegradation
Catabolism
Chains
Cholesterol
Cholesterol oxidase
Dehydrogenase
Dehydrogenases
Enzymes
Microbiology
Microorganisms
NAD
Nuclei
Oxidation
Oxygen
Rhodococcus
Sterols
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Summary:AbstractAn 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.Microbial sterol catabolism is initiated by conversion of 3β-ol-5-en into the corresponding 3-keto-4-en feature by either cholesterol oxidase requiring molecular oxygen or a NAD(P)-dependent dehydrogenase.
ISSN:0378-1097
1574-6968
DOI:10.1093/femsle/fnx007