TY - JOUR TI - A widely distributed metalloenzyme class enables gut microbial metabolism of host- and diet-derived catechols AU - Maini Rekdal, Vayu AU - Nol Bernadino, Paola AU - Luescher, Michael U AU - Kiamehr, Sina AU - Le, Chip AU - Bisanz, Jordan E AU - Turnbaugh, Peter J AU - Bess, Elizabeth N AU - Balskus, Emily P A2 - Weigel, Detlef A2 - Ley, Ruth Emily VL - 9 PY - 2020 DA - 2020/02/18 SP - e50845 C1 - eLife 2020;9:e50845 DO - 10.7554/eLife.50845 UR - https://doi.org/10.7554/eLife.50845 AB - 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. KW - Eggerthella lenta KW - Gordonibacter sp. KW - molybdenum enzyme KW - catechol dehydroxylase JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -