Enantiocomplementary Gut Bacterial Enzymes Metabolize Dietary Polyphenols.

ABSTRACT: Molybdenum-dependent catechol dehydroxylases in gut Actinobacteria catalyze the removal of para-hydroxyl groups from catechols, a central reaction in the microbial metabolism of polyphenol compounds. However, the substrates of most putative catechol dehydroxylases remain unidentified due to the challenges of obtaining these enzymes from standard heterologous expression systems. In this work, we establish Gordonibacter urolithinfaciens as a versatile bacterial host to express active catechol dehydroxylases. Using this system, we rapidly deorphanize eight previously uncharacterized gut bacterial catechol dehydroxylases that selectively dehydroxylate intermediates in the gut bacterial metabolism of plant-derived catechins and lignans. Unexpectedly, we discover multiple instances

SUBMITTER: Dong X 

PROVIDER: S-EPMC11887054 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature