A Distinct MaoC-like Enoyl-CoA Hydratase Architecture Mediates Cholesterol Catabolism in Mycobacterium tuberculosis

@inproceedings{Yang2014ADM,
  title={A Distinct MaoC-like Enoyl-CoA Hydratase Architecture
Mediates Cholesterol Catabolism in Mycobacterium tuberculosis},
  author={Meng Yang and Kip E. Guja and Suzanne T. Thomas and Miguel Garcia-Diaz and Nicole S Sampson},
  booktitle={ACS chemical biology},
  year={2014}
}
The Mycobacterium tuberculosis (Mtb) igr operon plays an essential role in Mtb cholesterol metabolism, which is critical for pathogenesis during the latent stage of Mtb infection. Here we report the first structure of a heterotetrameric MaoC-like enoyl-CoA hydratase, ChsH1-ChsH2, which is encoded by two adjacent genes from the igr operon. We demonstrate that ChsH1-ChsH2 catalyzes the hydration of a steroid enoyl-CoA, 3-oxo-4,17-pregnadiene-20-carboxyl-CoA, in the modified β-oxidation pathway… CONTINUE READING
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