In this study, benzoconduritols, benzohalogenoconduritol, and benzodihalogenoconduritols with conduritol-A and –C structures from oxo-norbornene derivative endo-10 b, exo-11 b cleavaged by Lewis acids (BBr3, BCl3, BF3· OEt2) and Ac2O/H2SO4 were defined. These compounds (10a, 24, 25, 26, 27, 28, 29, 34, and 35) have been evaluated for their potential to inhibit the α-glucosidase enzyme against acarbose-positive control. Among the compounds, halogen-substituted compounds 24, 25, 27, and 34 showed potent inhibition of the α-glucosidase enzyme compared with acarbose, while other compounds showed moderate inhibition. The kinetic studies of the most active compounds 24, 25, 27, and 34 were evaluated, then determined that they were mixed, non-competitive, and competitive type inhibitors. In addition, the in vitro cytotoxicity activities of these compounds were tested against human breast (BT-20), melanoma (SK-MEL128), prostate (DU-145), liver (SNU-398), lung (A549) cancer, and normal human fibroblast (HFC) cell lines. Among these compounds, the dichloro-substituted compound 25 showed the highest cytotoxic effect in the range of CC50 = 11.5–31.6 μg/mL against SNU-398, DU-145, SK-MEL128, A549, and HFC cell lines. The experimentally determined α-glucosidase and anticancer activity were studied by docking studies to demonstrate the binding orientation and interaction of the synthesized compound with amino acid residues present in the active site of human Maltase–Glucoamylase, topoisomerase II alpha, and Anaplastic Lymphoma Kinase enzymes.