Molybdoenzyme that catalyzes the anaerobic hydroxylation of a tertiary carbon atom in the side chain of cholesterol

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Abstract

Background: Cholesterol degradation is challenging due to its complex structure and low water solubility. Results: C25 dehydrogenase is a novel molybdenum/iron-sulfur/heme-containing enzyme that hydroxylates the tertiary C25 of the steroid side chain. Conclusion: C25 dehydrogenase and related enzymes identified in the genome of Sterolibacterium denitrificans replace oxygenases in anaerobic and even aerobic steroid metabolism. Significance: O2-independent hydroxylations by molybdoenzymes probably represent a general strategy to activate steroid substrates anaerobically. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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Dermer, J., & Fuchs, G. (2012). Molybdoenzyme that catalyzes the anaerobic hydroxylation of a tertiary carbon atom in the side chain of cholesterol. Journal of Biological Chemistry, 287(44), 36905–36916. https://doi.org/10.1074/jbc.M112.407304

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