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Gene Review

Nat1  -  N-acetyl transferase 1

Mus musculus

Synonyms: Aac1, Arylamide acetylase 1, Arylamine N-acetyltransferase 1, N-acetyltransferase type 1, NAT-1, ...
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Disease relevance of Nat1


High impact information on Nat1


Biological context of Nat1


Anatomical context of Nat1


Associations of Nat1 with chemical compounds

  • As expected, N-acetylation activity was undetectable in tissue cytosol preparations from Nat1/2(-/-) mice for 4-aminobiphenyl (ABP) and 2-aminofluorene (AF), whereas significant levels were measured in all wild-type tissue cytosols tested, indicating the widespread metabolism of these agents [6].
  • Longitudinal distribution of NATs in the intestine of the hamster, mouse, and two strains of rat was examined utilizing the model arylamine substrates procainamide(PA) and p-aminobenzoic acid (PABA) for the monomorphic (NAT1) and polymorphic (NAT2) enzymes in the rodent [10].
  • Intrinsic clearances for recombinant mouse NAT1- and NAT2-catalyzed N-acetylation of aromatic amine carcinogens were comparable [8].
  • A covalent, catalytic intermediate of cytosolic liver acetyl coenzyme A: arylamine N-acetyltransferase (EC from rapid acetylator rabbits (III/J) was isolated and chemically characterized [12].
  • Unlike young mature rats, the TH responsiveness of NAT-1 mRNA in both the cerebral and hepatic tissue of aged rats was blunted [11].

Other interactions of Nat1

  • In wild-type mice, NAT1 and NAT2 transcripts were detectable by RT-PCR in all tissues assayed including liver, kidney, colon, brain, bladder, and spleen [5].
  • Cloning, sequencing, and recombinant expression of NAT1, NAT2, and NAT3 derived from the C3H/HeJ (rapid) and A/HeJ (slow) acetylator inbred mouse: functional characterization of the activation and deactivation of aromatic amine carcinogens [8].

Analytical, diagnostic and therapeutic context of Nat1

  • Nat1- and Nat2-specific mRNA, determined by quantitative real-time polymerase chain reaction, was detected in all tissues examined and did not differ significantly (p > 0.05) between Nat2 KO and WT mice [13].


  1. Developmental expression of N-acetyltransferases in C57BI/6 mice. Mitchell, M.K., Futscher, B.W., McQueen, C.A. Drug Metab. Dispos. (1999) [Pubmed]
  2. Essential role of NAT1/p97/DAP5 in embryonic differentiation and the retinoic acid pathway. Yamanaka, S., Zhang, X.Y., Maeda, M., Miura, K., Wang, S., Farese, R.V., Iwao, H., Innerarity, T.L. EMBO J. (2000) [Pubmed]
  3. Two efficiency elements flanking the editing site of cytidine 6666 in the apolipoprotein B mRNA support mooring-dependent editing. Hersberger, M., Innerarity, T.L. J. Biol. Chem. (1998) [Pubmed]
  4. Aloe-emodin inhibited N-acetylation and DNA adduct of 2-aminofluorene and arylamine N-acetyltransferase gene expression in mouse leukemia L 1210 cells. Chung, J.G., Li, Y.C., Lee, Y.M., Lin, J.P., Cheng, K.C., Chang, W.C. Leuk. Res. (2003) [Pubmed]
  5. Generation and functional characterization of arylamine N-acetyltransferase Nat1/Nat2 double-knockout mice. Sugamori, K.S., Wong, S., Gaedigk, A., Yu, V., Abramovici, H., Rozmahel, R., Grant, D.M. Mol. Pharmacol. (2003) [Pubmed]
  6. In vivo and in vitro metabolism of arylamine procarcinogens in acetyltransferase-deficient mice. Sugamori, K.S., Brenneman, D., Grant, D.M. Drug Metab. Dispos. (2006) [Pubmed]
  7. Arylamine N-acetyltransferase from chicken liver. I. Monoclonal antibodies, immunoaffinity purification, and amino acid sequences. Deguchi, T., Sakamoto, Y., Sasaki, Y., Uyemura, K. J. Biol. Chem. (1988) [Pubmed]
  8. Cloning, sequencing, and recombinant expression of NAT1, NAT2, and NAT3 derived from the C3H/HeJ (rapid) and A/HeJ (slow) acetylator inbred mouse: functional characterization of the activation and deactivation of aromatic amine carcinogens. Fretland, A.J., Doll, M.A., Gray, K., Feng, Y., Hein, D.W. Toxicol. Appl. Pharmacol. (1997) [Pubmed]
  9. Spermidine/spermine n(1)-acetyltransferase catalyzes amantadine acetylation. Bras, A.P., Jänne, J., Porter, C.W., Sitar, D.S. Drug Metab. Dispos. (2001) [Pubmed]
  10. Longitudinal distribution of arylamine N-acetyltransferases in the intestine of the hamster, mouse, and rat. Evidence for multiplicity of N-acetyltransferases in the intestine. Ware, J.A., Svensson, C.K. Biochem. Pharmacol. (1996) [Pubmed]
  11. Novel translational repressor (NAT-1) expression is modified by thyroid state and age in brain and liver. Shah, G.N., Li, J., Mooradian, A.D. Eur. J. Endocrinol. (1998) [Pubmed]
  12. On the active site of liver acetyl-CoA. Arylamine N-acetyltransferase from rapid acetylator rabbits (III/J). Andres, H.H., Klem, A.J., Schopfer, L.M., Harrison, J.K., Weber, W.W. J. Biol. Chem. (1988) [Pubmed]
  13. N-acetyltransferase (nat) 1 and 2 expression in nat2 knockout mice. Loehle, J.A., Cornish, V., Wakefield, L., Doll, M.A., Neale, J.R., Zang, Y., Sim, E., Hein, D.W. J. Pharmacol. Exp. Ther. (2006) [Pubmed]
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