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- W2791046952 abstract "Significance All steroid-degrading bacteria utilize IpdAB, a predicted CoA transferase (CoT) that has been implicated in the hydrolysis of a carbon–carbon bond, an unprecedented reaction in CoTs. In Mycobacterium tuberculosis , IpdAB is required for degrading host cholesterol and virulence. We used a combination of X-ray crystallographic and biochemical studies to elucidate the mechanism of IpdAB. Superposition of the IpdAB Mtb active site with those of CoTs reveals distinct architectural features which, in conjunction with the biochemical data, indicate that IpdAB catalyzes a retro-Claisen-like ring-opening reaction. This reaction is unique for a member of the CoT superfamily. This study provides insights into bacterial steroid catabolism and facilitates the development of potential antituberculosis therapeutics targeting IpdAB." @default.
- W2791046952 created "2018-03-29" @default.
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- W2791046952 date "2018-03-26" @default.
- W2791046952 modified "2023-09-26" @default.
- W2791046952 title "IpdAB, a virulence factor in <i>Mycobacterium tuberculosis</i> , is a cholesterol ring-cleaving hydrolase" @default.
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- W2791046952 doi "https://doi.org/10.1073/pnas.1717015115" @default.
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