Liu Dafeng, Du Yanyan, Abdiriyim Ablikim, Zhang Lvxia, Song Daoqi, Deng Huashui, Wen Xiongying, Zhang Yanyan, Sun Bingwang
Xinjiang Key Laboratory of Lavender Conservation and Utilization, College of Biological Sciences and Technology, Yili Normal University, Yining, Xinjiang, China.
School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
Front Chem. 2025 Jun 11;13:1627286. doi: 10.3389/fchem.2025.1627286. eCollection 2025.
Volatile esters are key flavor components in most plants, including (lavandin). The final step in ester biosynthesis is catalyzed by alcohol acyltransferases (LiAATases), which attach alcohols to acyl groups. However, the functional role and mechanism of LiAATases remain poorly understood. Here, we predicted their structural models using AlphaFold2 and identified potential active site residues through the GalaxyWEB program. Catalytic assays were optimized at pH 7.5 and 30 °C. Substrate specificity for alcohols was assessed for both enzymes. Gene expression analysis revealed that and were most highly expressed in the petals and pistils, respectively, with peak expression occurring at stage 4 for and stage 1 for . Our study aims to elucidate the functional properties of alcohol acyltransferases in , contributing to an understanding of ester biosynthesis and specificity in this species.
挥发性酯类是大多数植物(包括熏衣草)中的关键风味成分。酯生物合成的最后一步由醇酰基转移酶(LiAATases)催化,该酶将醇与酰基结合。然而,LiAATases的功能作用和机制仍知之甚少。在这里,我们使用AlphaFold2预测了它们的结构模型,并通过GalaxyWEB程序鉴定了潜在的活性位点残基。在pH 7.5和30°C条件下优化了催化测定。评估了两种酶对醇的底物特异性。基因表达分析表明,[具体基因1]和[具体基因2]分别在花瓣和雌蕊中表达最高,[具体基因1]在第4阶段达到表达峰值,[具体基因2]在第1阶段达到表达峰值。我们的研究旨在阐明熏衣草中醇酰基转移酶的功能特性,有助于了解该物种的酯生物合成和特异性。