Analysis of the Expression Profiles of Borneol Dehydrogenase Genes and Its Catalytic Function in Camphor Biosynthesis in Lavender

"Xinxun 4", correlating with its highest camphor content. Subcellular localization showed BDH1 resides in the cytoplasm, suggesting plastid-cytoplasm collaboration. In vitro assays demonstrated that BDH1 and BDH2 both oxidize (+)- and (-)-borneol to camphor. Molecular dynamics simulations revealed that BDH1's active site exhibits conformational flexibility, accommodating both enantiomers with similar binding affinities, which was confirmed by enzyme kinetics. Asn90 was identified as a key catalytic residue. These findings reveal BDH family expansion, coordinated gene expression driving camphor accumulation, and BDH1's catalytic flexibility, offering key genetic resources and mechanistic insights for optimizing lavender camphor content via metabolic engineering and molecular breeding.