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

Yue Wang, Qian Wang, Chunlei Wang, Pengchao Wang, Ran Wang, Jing Wu, Hirokazu Kawagishi, Chengwei Liu

Abstract read

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Article in Natural products and bioprospecting, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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8 authors.

Yue WangState Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin, 150040, China.

Qian WangState Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin, 150040, China.

Chunlei WangState Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin, 150040, China.

Pengchao WangState Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin, 150040, China.

Ran WangCollege of Food and Biotechnology, Changchun Polytechnic University, Changchun, 130033, China.

Jing WuFaculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka, 020-8550, Japan.

Hirokazu KawagishiFaculty of Agriculture and Research Institute of Mushroom Science, Shizuoka University, Shizuoka, 422-8529, Japan.

Chengwei LiuState Key Laboratory of Utilization of Woody Oil Resource, College of Life Science, Northeast Forestry University, Harbin, 150040, China. liuchw@nefu.edu.cn.ORCID http://orcid.org/0000-0003-2746-2080

Funding

National Natural Science Foundation of China 32370069National Natural Science Foundation of China U22A20369Natural Science Foundation of Tianjin Municipal Science and Technology Commission JCYJ20240813151816022Science Fund for Distinguished Young Scholars of Heilongjiang Province LH2023C035

6 · The paper itself

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.

Indexed as

Aspergillus oryzaeHeterologous expressionLaetiporus sulphureusTargeted mutationUbiA prenyltransferase

Identifiers

PMID41520076

DOI10.1007/s13659-025-00571-2

PMCPMC12790560

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