2310038E17Rik Activators

Chemical activators of carboxylesterase 2F include a variety of compounds that engage the enzyme in different ways to enhance its activity. Acetylcholine, for example, is known to bind cholinergic receptors, leading to a signaling cascade that can culminate in increased enzymatic activity of carboxylesterase 2F, essentially priming the enzyme for action upon its substrates. Similarly, butyrylcholine, while being hydrolyzed by carboxylesterases, serves as a substrate that can lead to an activation of carboxylesterase 2F, effectively increasing the enzyme's turnover rate. This substrate-like activation is also seen with compounds such as procaine and cocaine, both of which are metabolized by carboxylesterase 2F and thus directly engage and activate the enzyme's hydrolytic function.

Other chemicals, such as rivastigmine, methylphenidate, and remoxipride, are metabolized by carboxylesterases and can indirectly increase the functional activity of carboxylesterase 2F by ensuring a steady supply of substrates for the enzyme to act upon. This metabolic demand for hydrolysis can serve as an impetus for the activation of carboxylesterase 2F, ensuring that it remains in an active state to process these compounds. Aspirin, also known as acetylsalicylic acid, undergoes hydrolysis by carboxylesterase 2F, which in turn leads to the functional activation of the enzyme. This process is a direct activation mechanism, as the enzyme is engaging with the substrate itself to perform its catalytic function. Clopidogrel, another compound processed by carboxylesterase 2F into its active metabolite, activates the enzyme in a similar fashion, highlighting the role of carboxylesterase 2F in drug metabolism. Dibucaine and prilocaine further exemplify the capacity of carboxylesterase 2F to act on various substrates; their hydrolysis by the enzyme directly enhances its activity, demonstrating the enzyme's broad substrate specificity and its ability to be activated by a diverse array of chemical entities.