Discovering a mitochondrion-localized BAHD acyltransferase involved in calystegine biosynthesis and engineering the production of 3β-tigloyloxytropane

文献类型： 外文期刊

第一作者： Zeng, Junlan

作者： Zeng, Junlan;Liu, Xiaoqiang;Zhang, Fangyuan;Qiu, Fei;Zhong, Mingyu;Zhao, Tengfei;Yang, Chunxian;Zeng, Lingjiang;Tang, Kexuan;Liao, Zhihua;Dong, Zhaoyue;Chen, Min;Lan, Xiaozhong;Zhang, Hongbo;Zhou, Junhui;Tang, Kexuan

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期刊名称：NATURE COMMUNICATIONS （ 影响因子：14.7； 五年影响因子：16.1 ）

ISSN：

年卷期： 2024 年 15 卷 1 期

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收录情况： SCI

摘要： Solanaceous plants produce tropane alkaloids (TAs) via esterification of 3 alpha- and 3 beta-tropanol. Although littorine synthase is revealed to be responsible for 3 alpha-tropanol esterification that leads to hyoscyamine biosynthesis, the genes associated with 3 beta-tropanol esterification are unknown. Here, we report that a BAHD acyltransferase from Atropa belladonna, 3 beta-tigloyloxytropane synthase (TS), catalyzes 3 beta-tropanol and tigloyl-CoA to form 3 beta-tigloyloxytropane, the key intermediate in calystegine biosynthesis and a potential drug for treating neurodegenerative disease. Unlike other cytosolic-localized BAHD acyltransferases, TS is localized to mitochondria. The catalytic mechanism of TS is revealed through molecular docking and site-directed mutagenesis. Subsequently, 3 beta-tigloyloxytropane is synthesized in tobacco. A bacterial CoA ligase (PcICS) is found to synthesize tigloyl-CoA, an acyl donor for 3 beta-tigloyloxytropane biosynthesis. By expressing TS mutant and PcICS, engineered Escherichia coli synthesizes 3 beta-tigloyloxytropane from tiglic acid and 3 beta-tropanol. This study helps to characterize the enzymology and chemodiversity of TAs and provides an approach for producing 3 beta-tigloyloxytropane.

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