Integrative Biology Journals

Natural Products and Bioprospecting ›› 2026, Vol. 16 ›› Issue (2): 17-17.DOI: 10.1007/s13659-025-00571-2

• ORIGINAL ARTICLES •     Next Articles

Genome mining reveals the unique function of UbiA-type prenyltransferase in Laetiporus sulphureus

Yue Wang1, Qian Wang1, Chunlei Wang1, Pengchao Wang1, Ran Wang2, Jing Wu3, Hirokazu Kawagishi4, Chengwei Liu1   

  1. 1. State Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin 150040, China;
    2. College of Food and Biotechnology, Changchun Polytechnic University, Changchun 130033, China;
    3. Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan;
    4. Faculty of Agriculture and Research Institute of Mushroom Science, Shizuoka University, Shizuoka 422-8529, Japan
  • Received:2025-07-15 Online:2026-04-22 Published:2026-04-22
  • Contact: Chengwei Liu,Email:liuchw@nefu.edu.cn
  • Supported by:
    National Natural Science Foundation of China, 32370069, Chengwei Liu, U22A20369, Chengwei Liu, Science Fund for Distinguished Young Scholars of Heilongjiang Province, LH2023C035, Chengwei Liu, Natural Science Foundation of Tianjin Municipal Science and Technology Commission, JCYJ20240813151816022, Chengwei Liu.

Genome mining reveals the unique function of UbiA-type prenyltransferase in Laetiporus sulphureus

Yue Wang1, Qian Wang1, Chunlei Wang1, Pengchao Wang1, Ran Wang2, Jing Wu3, Hirokazu Kawagishi4, Chengwei Liu1   

  1. 1. State Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin 150040, China;
    2. College of Food and Biotechnology, Changchun Polytechnic University, Changchun 130033, China;
    3. Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan;
    4. Faculty of Agriculture and Research Institute of Mushroom Science, Shizuoka University, Shizuoka 422-8529, Japan
  • 通讯作者: Chengwei Liu,Email:liuchw@nefu.edu.cn
  • 基金资助:
    National Natural Science Foundation of China, 32370069, Chengwei Liu, U22A20369, Chengwei Liu, Science Fund for Distinguished Young Scholars of Heilongjiang Province, LH2023C035, Chengwei Liu, Natural Science Foundation of Tianjin Municipal Science and Technology Commission, JCYJ20240813151816022, Chengwei Liu.

Abstract: Eight UbiA-type prenyltransferases were mined in Laetiporus sulphureus by bioinformatic analysis, and phylogenetic analysis showed that they have unique functions. Through heterologous expression in Aspergillus oryzae and addition of exogenous hydroquinone (HYQ, 2) substrate, it was found that LaPT3 could transfer isoprenyl groups on 2. Substrate specificity studies revealed that LaPT3 was substrate specific and could only transfer dimethylallyl diphosphate (DMAPP) using 2 as substrate to produce the product 2-(3-methylbut-2-en-1-yl) benzene-1,4-diol (1). The key active sites of LaPT3 were analyzed and two key amino acid sites near the conserved motifs were targeted for mutation, and the product yields were reduced to 60% and 29% respectively by mutating N100 to S and G208 to A. Molecular docking and site-directed mutagenesis results indicate that these two amino acid sites play a crucial role in the catalytic generation of 2 by LaPT3 to produce 1.

Key words: Laetiporus sulphureus, UbiA prenyltransferase, Heterologous expression, Targeted mutation, Aspergillus oryzae

摘要: Eight UbiA-type prenyltransferases were mined in Laetiporus sulphureus by bioinformatic analysis, and phylogenetic analysis showed that they have unique functions. Through heterologous expression in Aspergillus oryzae and addition of exogenous hydroquinone (HYQ, 2) substrate, it was found that LaPT3 could transfer isoprenyl groups on 2. Substrate specificity studies revealed that LaPT3 was substrate specific and could only transfer dimethylallyl diphosphate (DMAPP) using 2 as substrate to produce the product 2-(3-methylbut-2-en-1-yl) benzene-1,4-diol (1). The key active sites of LaPT3 were analyzed and two key amino acid sites near the conserved motifs were targeted for mutation, and the product yields were reduced to 60% and 29% respectively by mutating N100 to S and G208 to A. Molecular docking and site-directed mutagenesis results indicate that these two amino acid sites play a crucial role in the catalytic generation of 2 by LaPT3 to produce 1.

关键词: Laetiporus sulphureus, UbiA prenyltransferase, Heterologous expression, Targeted mutation, Aspergillus oryzae