A widely distributed metalloenzyme class enables gut microbial metabolism of host-and diet-derived catechols

Vayu Maini Rekdal, Paola Nol Bernadino, Michael U. Luescher, Sina Kiamehr, Chip Le, Jordan E. Bisanz, Peter J. Turnbaugh, Elizabeth N. Bess, Emily P. Balskus

    Research output: Contribution to journalArticlepeer-review

    4 Scopus citations

    Abstract

    Catechol dehydroxylation is a central chemical transformation in the gut microbial metabolism of plant- and host-derived small molecules. However, the molecular basis for this transformation and its distribution among gut microorganisms are poorly understood. Here, we characterize a molybdenum-dependent enzyme from the human gut bacterium Eggerthella lenta that dehydroxylates catecholamine neurotransmitters. Our findings suggest that this activity enables E. lenta to use dopamine as an electron acceptor. We also identify candidate dehydroxylases that metabolize additional host- and plant-derived catechols. These dehydroxylases belong to a distinct group of largely uncharacterized molybdenum-dependent enzymes that likely mediate primary and secondary metabolism in multiple environments. Finally, we observe catechol dehydroxylation in the gut microbiotas of diverse mammals, confirming the presence of this chemistry in habitats beyond the human gut. These results suggest that the chemical strategies that mediate metabolism and interactions in the human gut are relevant to a broad range of species and habitats.

    Original languageEnglish (US)
    Article numbere50845
    JournaleLife
    Volume9
    DOIs
    StatePublished - Feb 2020

    All Science Journal Classification (ASJC) codes

    • Neuroscience(all)
    • Biochemistry, Genetics and Molecular Biology(all)
    • Immunology and Microbiology(all)

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