Unexpected roles of aromatic ring-cleaving dioxygenases in oxygen-heterocycle degradation: Functional diversity, gene redundancy, and ecological implications. (PubMed, Water Res) - Aug 7, 2026 - "By integrating affinity predictions with in vivo validation, we demonstrated that classical aromatic ring-cleaving dioxygenases, including the intradiol dioxygenases CatA1/CatA2 from Cupriavidus metallidurans ZM02 and the extradiol dioxygenase MhpB from Escherichia coli BL21, mediate the cellular cleavage of 2-hydroxytetrahydrofuran (2-OH THF), a key intermediate in THF metabolism, to yield 4-hydroxybutyric acid (GHB)...Furthermore, catA genes are frequently redundant in bacteria degrading both O-heterocycles and aromatics, and their active sites are highly conserved, suggesting an evolutionary conserved strategy for coping with mixed pollutants. These findings expand the substrate spectrum of well-known dioxygenases to include O-heterocycles, establish a novel catalytic route for cyclic ether degradation in aquatic systems, and offer new opportunities for bioremediation and enzyme engineering in water treatment."
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Ahmed Sayed Badawy; Christopher E French; Hao Ren; Meimei Cai; Siqing Fan; Xiangyu Kong; Yiran Yin; Zhenmei Lu
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