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This gene encodes a type of N-acetyltransferase. The NAT2 isozyme functions to both activate and deactivate arylamine and hydrazine drugs and carcinogens. Polymorphisms in this gene are responsible for the N-acetylation polymorphism in which human populations segregate into rapid, intermediate, and slow acetylatorphenotypes. Polymorphisms in NAT2 are also associated with higher incidences of cancer and drug toxicity. A second arylamine N-acetyltransferase gene (NAT1) is located near NAT2.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Vatsis KP, Weber WW, Bell DA, Dupret JM, Evans DA, Grant DM, Hein DW, Lin HJ, Meyer UA, Relling MV, Sim E, Suzuki T, Yamazoe Y (February 1995). "Nomenclature for N-acetyltransferases". Pharmacogenetics. 5 (1): 1–17. doi:10.1097/00008571-199502000-00001. PMID7773298.
^Agúndez JA (2008). "N-acetyltransferases: lessons learned from eighty years of research". Curr. Drug Metab. 9 (6): 463–4. doi:10.2174/138920008784892146. PMID18680465.
Vatsis KP, Weber WW, Bell DA, Dupret JM, Evans DA, Grant DM, Hein DW, Lin HJ, Meyer UA, Relling MV (1995). "Nomenclature for N-acetyltransferases". Pharmacogenetics. 5 (1): 1–17. doi:10.1097/00008571-199502000-00001. PMID7773298.
Windmill KF, McKinnon RA, Zhu X, Gaedigk A, Grant DM, McManus ME (1997). "The role of xenobiotic metabolizing enzymes in arylamine toxicity and carcinogenesis: functional and localization studies". Mutat. Res. 376 (1–2): 153–60. doi:10.1016/S0027-5107(97)00038-9. PMID9202751.
Lan Q, Rothman N, Chow WH, Lissowska J, Doll MA, Xiao GH, Zatonski W, Hein DW (2003). "No apparent association between NAT1 and NAT2 genotypes and risk of stomach cancer". Cancer Epidemiol. Biomarkers Prev. 12 (4): 384–6. PMID12692115.