期刊
MOLECULES
卷 26, 期 9, 页码 -出版社
MDPI
DOI: 10.3390/molecules26092779
关键词
Escherichia coli; biotransformation; sodium benzoate; benzoate-CoA ligase; benzophenone synthase; 2; 4; 6-trihydroxybenzophenone; structural annotation
资金
- Faculty of Pharmaceutical Sciences, Khon Kaen University, Thailand
- National Research Council of Thailand, Khon Kaen University, 2018 (NRCT-KKU 2018) [610034]
A new artificial pathway was established in E. coli to transform sodium benzoate into 2,4,6-trihydroxybenzophenone, paving the way for further syntheses of benzophenone derivatives by adding various catalytic genes for functional groups.
The synthesis of natural products by E. coli is a challenging alternative method of environmentally friendly minimization of hazardous waste. Here, we establish a recombinant E. coli 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 Rhodopseudomonas palustris (BadA) and benzophenone synthase from Garcinia mangostana (GmBPS). It was found that the engineered E. coli 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 E. coli 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据