ABHD4 Inhibitors

ABHD4 inhibitors encompass a variety of chemical entities that can interfere with the function of the ABHD4 enzyme. These inhibitors are not limited to a single structural class but include several types of compounds that can affect the enzyme's activity through different mechanisms. Many of these inhibitors are not specific to ABHD4 but belong to broader categories of enzyme inhibitors that target serine hydrolases or lipases, which are enzyme classes that ABHD4 is a part of. For instance, compounds like sulfonyl fluorides are known to form a covalent bond with the serine residue in the active site of serine hydrolases, which could lead to the inhibition of ABHD4 if it shares a similar mechanism of action with other serine hydrolases. Similarly, MAFP and its derivatives are irreversible inhibitors that target a wide range of serine hydrolases, suggesting that they may also inhibit ABHD4.

Moreover, some compounds, such as URB597, PF-3845, and JZL184, are designed to specifically inhibit fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MAGL), or other enzymes within the endocannabinoid system. Although these are not direct inhibitors of ABHD4, their action can result in altered levels of endocannabinoids and related lipid signaling molecules, which may indirectly impact ABHD4's activity within the same pathway. Other broad-spectrum inhibitors like THL (Tetrahydrolipstatin) can inhibit a range of lipases and could potentially inhibit ABHD4 due to its lipase-like activity. Betulinic Acid, a naturally occurring pentacyclic triterpenoid, has been shown to inhibit serine hydrolases, and although its influence on ABHD4 is not explicitly documented, its mode of action allows for the possibility of ABHD4 inhibition. These chemicals, through their interactions with lipid metabolic processes and serine hydrolase enzyme activities, can indirectly influence ABHD4 functionality within cellular contexts