Terpenes are vital plant secondary metabolites that contribute to chemical defense, mediate stress responses, and support cellular signaling. Terpene synthases (TPSs) generate diverse terpene scaffolds that are subsequently modified by cytochrome P450 monooxygenases (CYPs), expanding structural and functional diversity. In Medicago truncatula, a model legume, terpene synthase 10 (MtTPS10) is strongly upregulated in roots during infection by the oomycete pathogen Aphanomyces euteiches. Current laboratory work has identified two cytochrome P450 enzymes, CYP71D81 and CYP71D82, positioned within the putative biosynthetic region containing MtTPS10. Each enzyme independently catalyzes oxidative modifications of the MtTPS10-derived sesquiterpene himachalol, producing two distinct derivatives. Here, we characterize the activity and substrate specificity of these CYP enzymes using Nicotiana benthamiana through Agrobacterium-mediated transient expression. Resulting metabolites were analyzed by gas chromatography-mass spectrometry (GC-MS). Elucidating this biosynthetic pathway highlights how CYP-driven oxidative tailoring diversifies terpene structures and contributes to pathogen-induced plant metabolic defense mechanisms.