Nasetyylitransferaasit

Nasetyylitransferaasit, often abbreviated NATs, are a superfamily of enzymes found in a wide variety of organisms, including humans, bacteria, and plants. These enzymes play a crucial role in xenobiotic metabolism and detoxification. Their primary function is to catalyze the transfer of an acetyl group from acetyl-CoA to a diverse range of acceptor molecules, including drugs, toxins, and endogenous compounds. This acetylation process generally renders these substances more water-soluble, facilitating their excretion from the body.

In humans, NATs are particularly important for the metabolism of many therapeutic agents, such as isoniazid (used to treat tuberculosis), sulfonamides, and hydralazine. Polymorphisms in the genes encoding NAT enzymes, especially NAT1 and NAT2, are well-documented and can lead to significant inter-individual differences in drug response. Individuals can be classified as rapid, intermediate, or slow acetylators based on their genetic makeup, influencing their ability to metabolize certain drugs effectively and increasing their susceptibility to adverse drug reactions. Beyond drug metabolism, NATs are also involved in the acetylation of various endogenous substrates, contributing to cellular signaling and regulation.