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The aim of this paper is to further explore the enzymatic properties of two synthetic Schiff base compounds. The corresponding copper complex (Cu(L)), with its Schiff base ligand (HL) have been synthesized and their spectroscopic (IR, UV-visible., NMR (H,C, Dept-135) and MS), thermogravimetric (TG/DTG), electrochemical (CV) and theoretical (Density Functional Theory) using the hybrid B3LYP/6–31 G(d,p) method) properties have been studied and well discussed. The electrochemical behaviour of Cu(L) displays the Cu(III)/Cu(II) and Cu(lI)/Cu(I) redox processes. The molecular structure of HL is confirmed by X-ray diffraction analysis. HL crystalized in the triclinic system with the space group of P-1. The morphological structures are also analyzed by X-ray powder diffraction, scanning electron microscopy with energy-dispersive X-ray spectroscopy. To improve their biological activities, inhibition of the target proteins, acetylcholinesterase (AChE), butyrylcholinesterase (BChE), Tyrosinase (TYR), and Urease enzymes are tested in vitro and in silico using molecular docking. Furthermore, their ADMET parameters are analyzed. The drug-likeness results indicate that HL followed to Lipinski’s, Ghose’s, Veber’s, Egan’s and Muegge’s rules contrary to its copper complex which followed only to Veber’s rule. Due to the importance of cytochrome P450s proteins for detoxification, five major CYP isoforms (CYP1A2, CYP2C19, CYP2C9, CYP2D6, and CYP3A4) are also considered during in silico prediction.