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

## TL;DR

Researchers identified a unique UbiA-type prenyltransferase in Laetiporus sulphureus that catalyzes a specific chemical reaction using a particular substrate.

## Contribution

The study reveals the unique catalytic function of LaPT3 in L. sulphureus through genome mining and experimental validation.

## Key findings

- LaPT3 transfers isoprenyl groups on hydroquinone to produce 2-(3-methylbut-2-en-1-yl) benzene-1,4-diol.
- Mutating key amino acids N100 and G208 in LaPT3 significantly reduced product yield.
- Molecular docking and mutagenesis confirmed the critical role of these amino acids in catalysis.

## 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.

The online version contains supplementary material available at 10.1007/s13659-025-00571-2.