ArticleNPJ biofilms and microbiomes2025
The presence and induction of regioselective dehydroxylases dictate urolithin metabolism by Enterocloster species.
Article in NPJ biofilms and microbiomes, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- O-methylation of phenolic natural products: translational insights from resveratrol.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026Review
- How Gut Microbes Transform Dietary Phytonutrients: Enzymatic Pathways and Human Metabolite Exposure.Molecules (Basel, Switzerland) · 2026Review
- The microbiome-mitochondria axis: the context-dependent role of urolithin A in aging and cancer via mitophagy.Molecular biology reports · 2026Review
- Urolithins in clinical translation: from gut microbial metabolites to precision interventions.Frontiers in nutrition · 2026Review
- Distinct classes of gut bacterial molybdenum-dependent enzymes produce urolithins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Abstract
Urolithins are a class of bioactive metabolites derived from the metabolism of dietary ellagitannins by the human gut microbiota. In the gut, urolithins are dehydroxylated regioselectively based on microbiota composition and activity. A single 9-hydroxy urolithin dehydroxylase (ucd) operon in gut resident Enterocloster species has been described to date; however, most enzymes in the urolithin metabolic pathway remain uncharacterized. Here, we investigate urolithin cross-feeding between members of the gut microbiota and discover a novel urolithin dehydroxylase in a subset of Enterocloster species. We show that urolithin intermediates, released by gut resident Gordonibacter species during ellagic acid metabolism, are dehydroxylated at both the 9- and 10-positions by E. asparagiformis, E. citroniae, and E. pacaense, but not E. bolteae. Using untargeted proteomics, we uncover a 10-hydroxy urolithin dehydroxylase operon, termed uxd, responsible for these species-specific differences in urolithin metabolism. By inducing uxd expression with diverse urolithins, we show that 9-hydroxy urolithins are required for uxd transcription and 10-position dehydroxylation. Collectively, this study reveals some of the genes, proteins, and substrate features underlying differences in urolithin metabolism by the human gut microbiota.
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