| Summary: | The synthesis of natural products by <i>E. coli</i> is a challenging alternative method of environmentally friendly minimization of hazardous waste. Here, we establish a recombinant <i>E. coli</i> capable of transforming sodium benzoate into 2,4,6-trihydroxybenzophenone (2,4,6-TriHB), the intermediate of benzophenones and xanthones derivatives, based on the coexpression of benzoate-CoA ligase from <i>Rhodopseudomonas palustris</i> (BadA) and benzophenone synthase from <i>Garcinia mangostana</i> (GmBPS). It was found that the engineered <i>E. coli</i> accepted benzoate as the leading substrate for the formation of benzoyl CoA by the function of BadA and subsequently condensed, with the endogenous malonyl CoA by the catalytic function of BPS, into 2,4,6-TriHB. This metabolite was excreted into the culture medium and was detected by the high-resolution LC-ESI-QTOF-MS/MS. The structure was elucidated by in silico tools: Sirius 4.5 combined with CSI FingerID web service. The results suggested the potential of the new artificial pathway in <i>E. coli</i> to successfully catalyze the transformation of sodium benzoate into 2,4,6-TriHB. This system will lead to further syntheses of other benzophenone derivatives via the addition of various genes to catalyze for functional groups.
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