Arylamine N-acetyltransferases (NAT-1 and NAT-2) catalyze N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a wide array of drugs. Certain alleles causing high N-acetyltransferase activity have been associated with colon and urinary bladder cancers, as NATs also bioactivate several known carcinogens. Both NAT-1 and NAT-2 are cytoplasmic proteins and play an active role in the detoxification of many arylamine and hydrazine drugs. N-acetylation polymorphism is determined by the level of NAT activity in liver tissues, and has been linked to the action and toxicity of drugs that contain amines. Human NAT-1 is the functional homolog of rodent NAT-2, while human NAT-2 is the functional homolog of rodent NAT-1.
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Protein Aliases: Arylamide acetylase 1; Arylamine N-acetyltransferase 1; AT-1; MNAT; Monomorphic arylamine N-acetyltransferase; N(alpha)-acetyltransferase 15, NatA auxiliary subunit; N-acetyl transferase 1, liver, blood; N-acetyltransferase (arylamine N-acetyltransferase); N-acetyltransferase 1 (arylamine N-acetyltransferase); N-acetyltransferase type 1; NAT-1
Gene Aliases: AAC1; MNAT; Nat; NAT-1; NAT1; NATI