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A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia

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A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia

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PECK, Spencer C., Karin DENGER, Anna BURRICHTER, Stephania M. IRWIN, Emily P. BALSKUS, David SCHLEHECK, 2019. A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia. In: Proceedings of the National Academy of Sciences of the United States of America (PNAS). 116(8), pp. 3171-3176. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.1815661116

@article{Peck2019-02-19glycy-46846, title={A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia}, year={2019}, doi={10.1073/pnas.1815661116}, number={8}, volume={116}, issn={0027-8424}, journal={Proceedings of the National Academy of Sciences of the United States of America (PNAS)}, pages={3171--3176}, author={Peck, Spencer C. and Denger, Karin and Burrichter, Anna and Irwin, Stephania M. and Balskus, Emily P. and Schleheck, David} }

Schleheck, David Burrichter, Anna Balskus, Emily P. Schleheck, David 2019-09-12T13:28:34Z Irwin, Stephania M. Denger, Karin Peck, Spencer C. Denger, Karin A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia 2019-02-19 Balskus, Emily P. Peck, Spencer C. Burrichter, Anna Irwin, Stephania M. Attribution 4.0 International This paper describes a pathway for anaerobic bacterial metabolism of taurine (2-aminoethanesulfonate), an abundant substrate in the human intestinal microbiota, by the intestinal bacterium and opportunistic pathogen, Bilophila wadsworthia. This metabolism converts taurine to the toxic metabolite hydrogen sulfide (H<sub>2</sub>S), an activity associated with inflammatory bowel disease and colorectal cancer. A critical enzyme in this pathway is isethionate sulfite-lyase, a member of the glycyl radical enzyme family. This enzyme catalyzes a novel, radical-based C-S bond-cleavage reaction to convert isethionate (2-hydroxyethanesulfonate) to sulfite and acetaldehyde. This discovery improves our understanding of H<sub>2</sub>S production in the human body and may also offer new approaches for controlling intestinal H<sub>2</sub>S production and B. wadsworthia infections. 2019-09-12T13:28:34Z eng

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