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Newly identified essential amino acids affecting peanut (Arachis hypogaea L.) DGAT2 enzyme activity

文献类型： 外文期刊

作者： Peng, Zhenying 1 ; Zheng, Ling 2 ; Tian, Haiying 1 ; Wang, Jianguo 1 ; Liu, Wenwen 2 ; Meng, Jingjing 1 ; Zhang, Jialei 1 ; Li, Xinguo 1 ; Wan, Shubo 3 ;

作者机构： 1.Shandong Acad Agr Sci, Inst Crop Germplasm Resources, Jinan 250100, Peoples R China

2.Shandong Normal Univ, Coll Life Sci, Jinan 250014, Peoples R China

3.Shandong Acad Agr Sci, Jinan 250100, Peoples R China

关键词： DGAT; TAG biosynthesis; Enzyme activity; Fatty acid

期刊名称：HELIYON （ 影响因子：4.0； 五年影响因子：4.1 ）

ISSN：

年卷期： 2023 年 9 卷 1 期

页码：

收录情况： SCI

摘要： Triacylglycerols is the major storage lipid in most crop seeds. As the key enzyme catalyzing the final step of triacylglycerols biosynthesis, the activity of diacylglycerol acyltransferases directly related to oil content. It has been shown that certain amino acids are very important for enzyme activity, one amino acid variation will greatly change the enzyme activity. In this study, we identified three amino acid point mutations that affect the Arachis hypogaea diacylglycerol acyltransferase 2 enzyme activity, T107M, K251R and L316P. According to the three amino acid variations, three single-nucleotide-mutant sequences of Arachis hypogaea diacylglycerol acyl-transferase 2a were constructed and transformed into yeast strain H1246 for function verification. Results showed that T107M and K251R could change the fatty acid content and composition of the transformed yeast strains, whereas L316P led to the loss of enzyme activity. By analyzing the 2D and 3D structures of the three variants, we found that the changes of spatial structure of T107M, K251R and L316P caused the changes of the enzyme activity. Our study could provide a theoretical basis for changing the enzyme activity of DGAT by genetic engineering, and provide a new idea for increasing the oil content of the crops.

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