文献类型：期刊文献

英文题名：Genome-Wide Identification of Phenylacetaldehyde Reductase Genes and Molecular Docking Simulation Study of OePAR1 in Olives

作者：Fan, Yutong[1,2,3] Cui, Qizhen[1,2,3] Li, Shuyuan[1,2,3] Li, Yufei[1,2,3] Yi, Gang[1,2,3] Wang, Chenhe[1,2,3] Liu, Qingqing[1,2,3] Zhang, Jianguo[1,2,3] Rao, Guodong[1,2,3]

第一作者：Fan, Yutong

通信作者：Rao, GD[1];Rao, GD[2];Rao, GD[3]

机构：[1]Chinese Acad Forestry, Res Inst Forestry, State Key Lab Tree Genet & Breeding, Beijing 100091, Peoples R China;[2]Nanjing Forestry Univ, Collaborat Innovat Ctr Sustainable Forestry Southe, Nanjing 210037, Peoples R China;[3]Chinese Acad Forestry, Key Lab Tree Breeding & Cultivat, Natl Forestry & Grassland Adm, Res Inst Forestry, Beijing 100091, Peoples R China

年份：2025

卷号：16

期号：4

外文期刊名：FORESTS

收录：;EI(收录号：20251818319873);Scopus(收录号：2-s2.0-105003666832);WOS:【SCI-EXPANDED(收录号:WOS:001475008000001)】；

基金：This work was supported by Fundamental Research Funds of CAF (CAFYBB2023PA005-2, CAFYBB2021QC001) and National Natural Science Foundation of China (32371837).

语种：英文

外文关键词：gene family; hydroxytyrosol; oleuropein; Olea europaea; molecular docking

摘要：Hydroxytyrosol is a natural phenolic compound found in olives. Phenylacetaldehyde reductase (PAR) is a key enzyme in the final step of the hydroxytyrosol biosynthesis pathway in olives. However, genome-wide studies on the PAR gene family in olives have not been reported. In this study, 21 genes were identified through a genome-wide analysis. Phylogenetic analysis classified these genes into three subgroups: PAR, CCR (Cinnamoyl-CoA reductase), and DFR (Dihydroflavonol 4-reductase). Expression pattern analysis suggested that genes within these subfamilies may play crucial roles in the biosynthesis of polyphenols, lignin, and anthocyanins, respectively. Three-dimensional structural modeling and molecular docking of the OePAR1 revealed that hydrogen bonds, hydrophobic interactions, and pi-pi stacking interactions collectively influence the affinity between PAR and its substrates. Residues at the active site form hydrogen bonds, with variations contributing to substrate specificity. The substrate with the strongest affinity for OePAR1 was identified as 3,4-dihydroxyphenylacetaldehyde (3, 4-DHPAA), with a binding energy of -4.98 kcal/mol, in agreement with previous enzymatic activity validation. Subcellular localization studies revealed that OePAR1 is localized to the chloroplast. This study provides essential insights into the biological functions of OePARs in olives and lays the groundwork for enhancing olive oil quality through genetic engineering.