An Efficient Prephenate Dehydrogenase Gene for the Biosynthesis of L-tyrosine: Gene Mining, Sequence Analysis, and Expression Optimization
文献类型： 外文期刊
作者： Ji, Anying 1 ; Bao, Pengfei 1 ; Ma, Aimin 1 ; Wei, Xuetuan 1 ;
作者机构： 1.Huazhong Agr Univ, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
2.Huazhong Agr Univ, Shenzhen Inst Nutr & Hlth, Wuhan 430070, Peoples R China
3.Chinese Acad Agr Sci, Shenzhen Branch, Guangdong Lab Lingnan Modern Agr, Genome Anal Lab,Minist Agr,Agr Genom Inst Shenzhen, Shenzhen 518000, Peoples R China
关键词： Bacillus amyloliquefaciens; L-tyrosine; prephenate dehydrogenase; recombinant expression; sequence analysis; element regulation
期刊名称：FOODS （ 影响因子：5.2； 五年影响因子：5.5 ）
ISSN：
年卷期： 2023 年 12 卷 16 期
页码：
收录情况： SCI
摘要： L-tyrosine is a key precursor for synthesis of various functional substances, but the microbial production of L-tyrosine faces huge challenges. The development of new microbial chassis cell and gene resource is especially important for the biosynthesis of L-tyrosine. In this study, the optimal host strain Bacillus amyloliquefaciens HZ-12 was firstly selected by detecting the production capacity of L-tyrosine. Subsequently, the recombinant expression of 15 prephenate dehydrogenase genes led to the discovery of the best gene, Bao-tyrA from B. amyloliquefaciens HZ-12. After the overexpression of Bao-tyrA, the L-tyrosine yield of the recombinant strain HZ/P43-Bao-tyrA reach 411 mg/L, increased by 42% compared with the control strain (HZ/pHY300PLK). Moreover, the nucleic acid sequence and deduced amino acid sequence of the gene Bao-tyrA were analyzed, and their conservative sites and catalytic mechanisms were proposed. Finally, the expression of Bao-tyrA was regulated through a promoter and 5'-UTR sequence to obtain the optimal expression elements. Thereby, the maximum L-tyrosine yield of 475 mg/L was obtained from HZ/P43-UTR3-Bao-tyrA. B. amyloliquefaciens was applied for the first time to produce L-tyrosine, and the optimal prephenate dehydrogenase gene Bao-tyrA and corresponding expression elements were obtained. This study provides new microbial host and gene resource for the construction of efficient L-tyrosine chassis cells, and also lays a solid foundation for the production of various functional tyrosine derivatives.
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