EG13909 Inhibitors

Chemical inhibitors of EG13909 include a variety of compounds that target the functional aspects of this protein's enzymatic activity. Orlistat is one such inhibitor that acts by forming a covalent bond with the serine residue of gastric and pancreatic lipases, which share functional similarities with EG13909, leading to an inhibition of their activity and a consequent reduction in fat absorption. Ebelactone B also targets enzymes like EG13909, specifically inhibiting esterases and lipases by covalently binding to the serine residue within their active sites. This binding action results in a direct blockade of the enzyme's function. Another inhibitor, Palmitoyl-CoA, functions as a competitive inhibitor, occupying the active site and thus preventing the binding of natural substrates, which is a necessary step for the enzymatic function of EG13909.

Methyl arachidonyl fluorophosphonate and Diethyl p-nitrophenyl phosphate both act as irreversible inhibitors for serine hydrolases by covalently modifying the serine residue at the active site of these enzymes. Given that EG13909 belongs to this class of enzymes, its activity can be inhibited through a similar mechanism. Iso-OMPA targets cholinesterases and other esterases/lipases, and by extension, can inhibit EG13909 by occupying its active site. Inhibitors like JZL184 and URB602, although primarily known for their action on monoacylglycerol lipase, have the potential to inhibit EG13909 due to the structural and mechanistic similarities between the enzymes. PF-750, which is known to inhibit serine hydrolases including fatty acid amide hydrolase through covalent modification, suggests that EG13909's activity can be inhibited through a similar approach, considering the shared enzyme class and action mechanism. These inhibitors collectively employ covalent modification and competitive inhibition strategies to reduce the function of EG13909 by directly interacting with the protein's active site or by competing with its natural substrates, thus inhibiting its enzymatic activity.