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A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia
Abstract
Significance: 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 2 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 2 S production in the human body and may also offer new approaches for controlling intestinal H 2 S production and B. wadsworthia infections.
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“Moreover, radical desulfonation enzymology has been described (Peck et al., 2019; Dawson et al., 2021), and radical desulfonation chemistry for PFAS has been described (Niu et al., 2016).”
From Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances (2022) · cites this paper as Peck et al., 2019
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Characterization of Choline Trimethylamine-Lyase Expands the Chemistry of Glycyl Radical Enzymes
Craciun, S., Marks, J. A., & Balskus, E. P. (2014) · ACS Chemical Biology · doi:10.1021/cb500113p · Cited by 139
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Infection trains the host for microbiota-enhanced resistance to pathogens
Stacy, A., Andrade-Oliveira, V., McCulloch, J. A., Hild, B., Oh, J. H., Perez-Chaparro, P. J., Sim, C. K., Lim, A. I., Link, V. M., Enamorado, M., et al. (2021) · Cell · doi:10.1016/j.cell.2020.12.011 · Cited by 239
Wackett, L. P. (2022) · Microbial Biotechnology · doi:10.1111/1751-7915.13928 · Cited by 165
Effects of Hydrogen Sulfide on the Microbiome: From Toxicity to Therapy
Buret, A. G., Allain, T., Motta, J.-P., & Wallace, J. L. (2022) · Antioxidants & Redox Signaling · doi:10.1089/ars.2021.0004 · Cited by 151
Metadata
- Authors
- Peck, S. C., Denger, K., Burrichter, A., Irwin, S. M., Balskus, E. P., & Schleheck, D.
- Affiliations
- Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138;
- Department of Biology, University of Konstanz, D-78457 Konstanz, Germany;
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-02-04
- Volume
- 116
- Issue
- 8
- Pages
- 3171-3176
- ISSN
- 0027-8424
- 1091-6490
- PMC
- PMC6386719
- Cited by
- 194
- References
- 4
- Language
- en
- Funders
- Deutsche Forschungsgemeinschaft (SCHL1936/3-4)
- Bill and Melinda Gates Foundation (unknown (to DS))
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