ES22 Inhibitors

Chemical inhibitors of ES22 operate through various mechanisms to impede the protein's enzymatic function. Bis(4-nitrophenyl) phosphate and Tetraisopropyl pyrophosphoramide, for instance, directly inhibit ES22 activity by binding to the active site that is common to serine hydrolases. This binding prevents the protein from catalyzing its typical ester hydrolysis reactions. Methyl arachidonyl fluorophosphonate follows a similar route of inhibition; however, it distinguishes itself by covalently modifying the active site serine, which results in irreversible inactivation. Ethopropazine, another inhibitor, exerts its effect by occupying the active site of ES22, thereby preventing the enzyme from interacting with its intended substrates.

Further, PMSF and Paraoxon target ES22 by sulfonylating and phosphorylating the active site serine residue, respectively, leading to a permanent inhibition of the protein's esterase function. This mechanism is shared by organophosphates such as E600, Malaoxon, and DFP, all of which phosphorylate the serine residue, thus ensuring that ES22 cannot perform its catalytic role. Mipafox, by inactivating the serine residue, also ensures the enzyme's activity is halted. Dichlorvos operates via a similar phosphorylation mechanism, ensuring the inhibition of ES22. Lastly, Cresyl violet acetate, by binding to serine hydrolases like ES22, blocks the protein's catalytic activity, rounding out the arsenal of chemical inhibitors that manage to inhibit the function of ES22 through direct interaction with its active site or via irreversible modification of crucial amino acid residues necessary for its enzymatic activity.