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

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 env

SUBMITTER: Maini Rekdal V 

PROVIDER: S-EPMC7028382 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature