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Catalytic mechanism and engineering of aromatic prenyltransferase: A review

文献类型： 外文期刊

作者： Huang, Yaoguang 1 ; Liu, Juan 3 ; Yang, Bao 1 ;

作者机构： 1.Chinese Acad Sci, Guangdong Prov Key Lab Appl Bot, Key State Lab Plant Divers & Specialty Crops,South, Key Lab Natl Forestry & Grassland Adm Plant Conser, Guangzhou 510650, Peoples R China

2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China

3.Guangdong Acad Agr Sci, Rice Res Inst, Guangzhou 510640, Peoples R China

关键词： Aromatic prenyltransferase; Enzyme modification; Phenolic compounds; Heterologous expression; Rational design

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 313 卷

页码：

收录情况： SCI

摘要： The prenylation of aromatic compounds significantly enhances their metabolic stability and bioactivity. Prenyltransferases, as essential biocatalysts, facilitate the regioselective transfer of prenyl groups from donors to aromatic substrates. This review systematically summarizes recent progress in the rational engineering of prenyltransferases through protein-based strategies, critically evaluates current challenges, and outlines future research priorities. Firstly, we delineate the biosynthetic pathways of prenylated phenolic compounds, emphasizing the pivotal roles of prenyltransferases, and classify these enzymes according to the structural diversity of their aromatic acceptor molecules. Secondly, the current state of prenyltransferase biosynthesis by comparing their heterologous expression levels across diverse microbial hosts is discussed, highlighting key factors influencing catalytic efficiency. Furthermore, we dissect the molecular mechanisms governing prenyltransferase activity and propose innovative engineering approaches integrating artificial intelligence and deep learning to develop high-performance biocatalysts for industrial applications. Finally, we address unresolved challenges in this field, including suboptimal catalytic activity, narrow substrate specificity, and limitations in multi-enzyme cascade systems and immobilization techniques. This review offers strategic insights to guide the engineering and scalable application of prenyltransferases in synthetic biology and pharmaceutical innovation.

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