Arylamine N-acetyltransferase 1 (NAT1)

Arylamine N-acetyltransferase 1 (NAT1) is a cytosolic acetyltransferase enzyme responsible for catalyzing the transfer of an acetyl group from acetyl-CoA to a variety of arylamine and hydrazine compounds, including important drugs (e.g., isoniazid) and environmental carcinogens[3][4][7]. NAT1 is involved in the detoxification and metabolic activation of xenobiotics, as well as in endogenous folate catabolism[3][4][5]. The enzyme operates via a catalytic triad consisting of cysteine, histidine, and aspartate residues, unique to the NAT enzyme family[6]. NAT1 plays a significant role in pharmacogenetics due to variable genetic alleles affecting enzyme activity and patient drug responses. Overexpression of NAT1 is observed in a subset of breast cancers, implicating it in cancer cell proliferation and as a potential biomarker or therapeutic target in oncology[1][4]. Safety concerns include variation in enzyme activity leading to altered drug efficacy or toxicity, as well as roles in carcinogen processing and cancer progression[1][5].

Other names

N-acetyltransferase 1NAT1EC 2.3.1.5Blood group antigen (HGNC:7646)

N-acetylation: transfer of acetyl group from acetyl-CoA to arylamine or hydrazine substrates, resulting in drug inactivation or detoxification[3][4][6]; Metabolism of endogenous substrates in folate catabolism[4][5]