N-acyltransferase (NAT)

N-acyltransferases are a diverse family of enzymes that catalyze the transfer of an acyl group (such as acetyl, propionyl, or other acyl chains) from a donor molecule—typically acyl-CoA derivatives—to a nitrogen atom on an acceptor substrate, usually an amine. Prominent subclasses include Arylamine N-acetyltransferase (NAT; involved in the metabolism of drugs and carcinogens in humans), Glycine N-acyltransferase (GLYAT; important in the detoxification of organic acids), and Arylakylamine N-acetyltransferase (AANAT; involved in neurotransmitter metabolism and circadian rhythm). Human NAT enzymes (particularly NAT1 and NAT2) acetylate a wide variety of drugs and environmental chemicals, impacting their pharmacological and toxicological properties. NAT activity is characterized by genetic polymorphisms leading to variations in drug efficacy and toxicity. The N-acyltransferase family is highly conserved and functionally diverse, with relevance spanning pharmacology, toxicology, cancer biology, infectious disease, and metabolism.

Other names

NATArylamine N-acetyltransferaseArylamine acetyltransferaseAcyltransferaseAANAT (Arylakylamine N-acetyltransferase)GLYAT (Glycine N-acyltransferase)Acetyltransferase

Acetylation (or acylation) of primary amine drugs and metabolites, affecting their pharmacokinetics, activity, and toxicity\nInactivation/detoxification of toxic amines and carcinogens (by acetylation rendering them more excretable)\nIn some cases, activation of procarcinogens