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来自Astragalus membranaceus的区域特异性沙素乙转移酶的特性和基于结构的蛋白质工程

Linlin Wang¹, Zhihui Jiang², Jiahe Zhang¹

¹State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, 38 Xueyuan Road, Beijing, 100191, China.

Nature communications

|September 25, 2023

概括

研究人员发现了一种新的酶,AmAT7-3,来自Astragalus membranaceus,该酶可乙化肥素. 这种酶及其工程变体为修改生物活性天然产品提供了新的工具.

科学领域:

生物化学生物化学
自然产品化学自然产品化学
酶学是一种酶学.

背景情况:

乙化增强了许多天然产品的生物活性.
在天然产品中糖分的乙化还不太清楚.

研究的目的:

发现和描述一种来自Astragalus membranaceus的新型沙素乙转移酶.
阐明已识别的酶的催化机制和基质特异性.
设计用于生物活性沙因的特异性乙化变体.

主要方法:

逐步进行基因挖掘,以识别AmAT7-3.3酶.
进行X射线晶体学以确定AmAT7-3及其基质的复杂结构.
量子力学/分子力学 (QM/MM) 计算来分析催化机制.
半理性设计以创建酶变体.

主要成果:

鉴定出AmAT7-3是一种Xylose C3'/C4'-O-乙烯基转移酶,用于阿斯特拉加索酸IV.
晶体结构显示出一个由AADAG序列影响的大型活性口袋.
酶的区域特异性是由糖位和关键氨基酸的位置决定的 (A310,L290).
工程变体A310G和A310W分别表现出特定的C3'-O和C4'-O乙化.
AmAT7-3及其变体成功地乙化了其他生物活性氨酸.

结论:

这项研究扩大了对萨波宁乙转移酶的知识.
AmAT7-3及其工程变体为沙素乙化提供了高效的工具.
这些发现有助于理解自然产品修改中的酶机制.

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