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A series of halo-substituted mixed ester/amide-based analogues  4a-l  have been prepared as jack bean urease inhibitor, which showed good to excellent inhibition of enzyme activity. The role of halo-substituted benzoyl moieties and alkyl substituted anilines in urease inhibitory kinetics was also investigated. The alkyl-substituted anilines  1a–b  reacted with chloroacetyl chloride to afford intermediates  2a-b , which were then reacted with different halo-substituted benzoic acids  3a–f  to prepare the title compounds  4a-l . The chemical structures of final products  4a-l  were ascertained by FTIR,  1 H NMR,  13 C NMR, and mass spectra. The compound  4b  showed remarkable activity with IC 50 1.6 ± 0.2 nM, better than the standard thiourea having IC 50 472.1 ± 135.1 nM. The 2-chloro-substituted phenyl ring on one side of compound  4b  and 4-isopropyl-substituted benzene on the other side play an essential role in inhibition of urease activity. Lineweaver–Burk plots (kinetics study) indicated about  4b  derivative as a mixed type of inhibitor. The virtual screening performed against urease enzyme (PDBID 4H9M) showed that compounds  4b  and  4e  have binding energies of −7.8 and −7.9 Kcal/mol, respectively. Based upon our results, it was found that derivative  4b  is a highly potent urease inhibitor, better than the standard thiourea.

Enzyme Inhibitory Kinetics and Molecular Docking Studies of Halo-Substituted Mixed Ester/Amide-Based Derivatives as Jack Bean Urease Inhibitors