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Gene Review

AANAT  -  aralkylamine N-acetyltransferase

Homo sapiens

Synonyms: AA-NAT, Aralkylamine N-acetyltransferase, DSPS, SNAT, Serotonin N-acetyltransferase, ...
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Disease relevance of AANAT


High impact information on AANAT


Chemical compound and disease context of AANAT


Biological context of AANAT

  • In the AANAT gene we found 4 novel SNPs: 2 in the 5' flanking region, 1 in exon 4, and 1 in intron 3 [10].
  • Kinetics of AANAT extracted from 1E7 cells are the same as those of bacterially expressed hAANAT; both preparations of hAANAT are equally sensitive to the inhibitor CoA-S-N-acetyltryptamine [11].
  • We have found that the human AA-NAT gene spans approximately 2.5 kb, contains four exons, and is located at chromosome 17q25 [12].
  • Arylalkylamine N-acetyltransferase (AANAT) catalyzes the reaction of serotonin with acetyl-CoA to form N-acetylserotonin and plays a major role in the regulation of the melatonin circadian rhythm in vertebrates [13].
  • Given a previous proposal that AANAT can catalyze an alkyltransferase reaction in a conformationally altered active site relative to its acetyltransferase activity, it is possible that the two conformations of the bisubstrate analog observed crystallographically correspond to these alternative reaction pathways [14].

Anatomical context of AANAT

  • The specific concentration of hAANAT in homogenates is comparable to that of the night rat pineal gland [11].
  • As described here, a cell line (1E7) expressing human AANAT (hAANAT) has been developed to study the human enzyme [11].
  • AANAT mRNA is abundant in the pineal gland and retina, but not elsewhere; AANAT mRNA is uniformly distributed in the pineal gland, but is limited primarily to the photoreceptor outer segments in the retina [15].
  • This study establishes that AANAT messenger RNA (mRNA) and functional enzyme occurs within the pars tuberalis (PT) and to a lesser degree within the pars distalis (PD) of the sheep pituitary gland; expression in these tissues is approximately 1/15th (PT) and 1/300th (PD) of that in the ovine pineal gland [16].
  • The absence of AANAT suggests that in human gallbladder, HIOMT might be involved in the formation of 5-hydroxytryptamine products other than melatonin [17].

Associations of AANAT with chemical compounds

  • Activation of nicotinic and muscarinic acetylcholine receptors increased [Ca2+]i, but did not alter cAMP levels, AANAT activity or melatonin production [18].
  • Here, the significance of the phosphorylation of AANAT was studied using a semisynthetic enzyme in which a nonhydrolyzable phosphoserine/threonine mimetic, phosphonomethylenealanine (Pma), was incorporated at position 31 (AANAT-Pma31) [19].
  • In this study, mechanistic aspects of the AANAT-catalyzed alkyl transfer reaction were explored by employing CoASH and a series of N-haloacetyltryptamines that were also evaluated for their AANAT acetyltransferase inhibitory activities [20].
  • AANAT is known to undergo complex and rapid regulation by a subtle balance between extremely fast catabolism and protection against it, both due to serine phosphorylation [21].
  • Collectively, these results suggest that NE triggers Ca(2+) entry coupled to BK channels and that NE-induced Ca(2+) entry is important in the regulation of AANAT [22].

Other interactions of AANAT


Analytical, diagnostic and therapeutic context of AANAT


  1. Serotoninergic and melatoninergic systems are fully expressed in human skin. Slominski, A., Pisarchik, A., Semak, I., Sweatman, T., Wortsman, J., Szczesniewski, A., Slugocki, G., McNulty, J., Kauser, S., Tobin, D.J., Jing, C., Johansson, O. FASEB J. (2002) [Pubmed]
  2. Significant association of the arylalkylamine N-acetyltransferase ( AA-NAT) gene with delayed sleep phase syndrome. Hohjoh, H., Takasu, M., Shishikura, K., Takahashi, Y., Honda, Y., Tokunaga, K. Neurogenetics (2003) [Pubmed]
  3. Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus. Aisien, S.O., Hellmund, C., Walter, R.D. Parasitol. Res. (1996) [Pubmed]
  4. Design, synthesis and in vitro evaluation of novel benzo[b]thiophene derivatives as serotonin N-acetyltransferase (AANAT) inhibitors. Mesangeau, C., Yous, S., Chavatte, P., Ferry, G., Audinot, V., Boutin, J.A., Delagrange, P., Bennejean, C., Renard, P., Lesieur, D. Journal of enzyme inhibition and medicinal chemistry. (2003) [Pubmed]
  5. Regulation of AA-NAT and HIOMT gene expression by butyrate and cyclic AMP in Y79 human retinoblastoma cells. Wiechmann, A.F., Burden, M.A. J. Pineal Res. (1999) [Pubmed]
  6. Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Obsil, T., Ghirlando, R., Klein, D.C., Ganguly, S., Dyda, F. Cell (2001) [Pubmed]
  7. Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis. Ganguly, S., Gastel, J.A., Weller, J.L., Schwartz, C., Jaffe, H., Namboodiri, M.A., Coon, S.L., Hickman, A.B., Rollag, M., Obsil, T., Beauverger, P., Ferry, G., Boutin, J.A., Klein, D.C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Mechanism-based inhibition of the melatonin rhythm enzyme: pharmacologic exploitation of active site functional plasticity. Khalil, E.M., De Angelis, J., Ishii, M., Cole, P.A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  9. Melatonin and 5-methoxytryptophol (5-ML) in nervous and/or neurosensory structures of a gastropod mollusc (Helix aspersa maxima): synthesis and diurnal rhythms. Blanc, A., Vivien-Roels, B., Pévet, P., Attia, J., Buisson, B. Gen. Comp. Endocrinol. (2003) [Pubmed]
  10. Identification of single-nucleotide polymorphisms (SNPs) of human N-acetyltransferase genes NAT1, NAT2, AANAT, ARD1 and L1CAM in the Japanese population. Sekine, A., Saito, S., Iida, A., Mitsunobu, Y., Higuchi, S., Harigae, S., Nakamura, Y. J. Hum. Genet. (2001) [Pubmed]
  11. cAmp regulation of arylalkylamine N-acetyltransferase (AANAT, EC a new cell line (1E7) provides evidence of intracellular AANAT activation. Coon, S.L., Weller, J.L., Korf, H.W., Namboodiri, M.A., Rollag, M., Klein, D.C. J. Biol. Chem. (2001) [Pubmed]
  12. The human serotonin N-acetyltransferase (EC gene (AANAT): structure, chromosomal localization, and tissue expression. Coon, S.L., Mazuruk, K., Bernard, M., Roseboom, P.H., Klein, D.C., Rodriguez, I.R. Genomics (1996) [Pubmed]
  13. Substrate specificity and inhibition studies of human serotonin N-acetyltransferase. Ferry, G., Loynel, A., Kucharczyk, N., Bertin, S., Rodriguez, M., Delagrange, P., Galizzi, J.P., Jacoby, E., Volland, J.P., Lesieur, D., Renard, P., Canet, E., Fauchère, J.L., Boutin, J.A. J. Biol. Chem. (2000) [Pubmed]
  14. X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. Wolf, E., De Angelis, J., Khalil, E.M., Cole, P.A., Burley, S.K. J. Mol. Biol. (2002) [Pubmed]
  15. Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-acetyltransferase (EC Coon, S.L., Del Olmo, E., Young, W.S., Klein, D.C. J. Clin. Endocrinol. Metab. (2002) [Pubmed]
  16. Ovine arylalkylamine N-acetyltransferase in the pineal and pituitary glands: differences in function and regulation. Fleming, J.V., Barrett, P., Coon, S.L., Klein, D.C., Morgan, P.J. Endocrinology (1999) [Pubmed]
  17. The melatonin receptor subtype MT1 is expressed in human gallbladder epithelia. Aust, S., Thalhammer, T., Humpeler, S., Jäger, W., Klimpfinger, M., Tucek, G., Obrist, P., Marktl, W., Penner, E., Ekmekcioglu, C. J. Pineal Res. (2004) [Pubmed]
  18. Signal transduction and regulation of melatonin synthesis in bovine pinealocytes: impact of adrenergic, peptidergic and cholinergic stimuli. Schomerus, C., Laedtke, E., Olcese, J., Weller, J.L., Klein, D.C., Korf, H.W. Cell Tissue Res. (2002) [Pubmed]
  19. Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation. Zheng, W., Zhang, Z., Ganguly, S., Weller, J.L., Klein, D.C., Cole, P.A. Nat. Struct. Biol. (2003) [Pubmed]
  20. Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase. Zheng, W., Scheibner, K.A., Ho, A.K., Cole, P.A. Chem. Biol. (2001) [Pubmed]
  21. Characterization and regulation of a CHO cell line stably expressing human serotonin N-acetyltransferase (EC Ferry, G., Mozo, J., Ubeaud, C., Berger, S., Bertrand, M., Try, A., Beauverger, P., Mesangeau, C., Delagrange, P., Boutin, J.A. Cell. Mol. Life Sci. (2002) [Pubmed]
  22. Norepinephrine activates store-operated Ca2+ entry coupled to large-conductance Ca2+-activated K+ channels in rat pinealocytes. Lee, S.Y., Choi, B.H., Hur, E.M., Lee, J.H., Lee, S.J., Lee, C.O., Kim, K.T. Am. J. Physiol., Cell Physiol. (2006) [Pubmed]
  23. Isolation and mapping of a cosmid clone containing the human NAT2 gene. Franke, S., Klawitz, I., Schnakenberg, E., Rommel, B., Van de Ven, W., Bullerdiek, J., Schloot, W. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  24. Expression of melatonin synthesis genes is controlled by a circadian clock in the pike pineal organ but not in the trout. Coon, S.L., Bégay, V., Falcón, J., Klein, D.C. Biol. Cell (1998) [Pubmed]
  25. The ovine melatonin-related receptor: cloning and preliminary distribution and binding studies. Drew, J.E., Barrett, P., Williams, L.M., Conway, S., Morgan, P.J. J. Neuroendocrinol. (1998) [Pubmed]
  26. Expression and cellular localization of melatonin-synthesizing enzymes in the rat lens. Itoh, M.T., Takahashi, N., Abe, M., Shimizu, K. J. Pineal Res. (2007) [Pubmed]
  27. Thiolsubtilisin acts as an acetyltransferase in organic solvents. Tai, D.F., Liaw, W.C. FEBS Lett. (2002) [Pubmed]
  28. Characterization of human melatonin synthesis using autoptic pineal tissue. Ackermann, K., Bux, R., Rüb, U., Korf, H.W., Kauert, G., Stehle, J.H. Endocrinology (2006) [Pubmed]
  29. High-capacity screening of arylalkylamine N-acetyltransferase inhibitors using a high-performance liquid chromatography system. Ferry, G., Boutin, J.A. Journal of biomolecular screening : the official journal of the Society for Biomolecular Screening. (2000) [Pubmed]
  30. Duality of serotonin-N-acetyltransferase in the gilthead seabream (Sparus aurata): molecular cloning and characterization of recombinant enzymes. Zilberman-Peled, B., Benhar, I., Coon, S.L., Ron, B., Gothilf, Y. Gen. Comp. Endocrinol. (2004) [Pubmed]
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