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Namboodiri, M.A.A.; Dubbels, R.; Klein, D.C.: Arylalkylamine N-acetyltransferase from mammalian pineal gland. Methods Enzymol., 142, 583–590 (1987)
Voisin, P.; Namboodiri, M.A.A.; Klein, D.C.: Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland. J. Biol. Chem., 259, 10913–10918 (1984)
Withyachumnarnkul, B.; Pongsa-Asawapaiboon, A.; Poolsanguan, B.: Characteristics of the enzyme N-acetyltransferase in the optic lobe of the giant freshwater prawn, Macrobrrachium rosenbergii. Comp. Biochem. Physiol. B Comp. Biochem., 104, 449–454 (1993)
Namboodiri, M.A.A.; Brownstein, M.J.; Voisin, P.; Weller, J.L.; Klein, D.C.: A simple and rapid method for the purification of ovine pineal arylalkylamine N-acetyltransferase. J. Neurochem., 48, 580–585 (1987)
Ohtomi, M.; Sasaki, M.; Deguchi, T.: Two arylamine N-acetyltransferases from chicken pineal gland as identified by cDNA cloning. Eur. J. Biochem., 185, 253–261 (1989)
Fajardo, N.; Abreu, P.; Alonso, R.: Determination of kinetic properties of serotonin-N-acetyltransferase in bovine pineal gland using HPLC with fluorimetric detection. J. Pineal Res., 13, 80–84 (1992)
Rodriguez-Cabello, J.C.; Agapito, M.T.; Garcia-Herrero, I.; Recio, J.M.: Effects of EGTA and calmodulin, neutral thiol proteinases and protein kinase C inhibitors on loss of chicken pineal serotonin N-acetyltransferase activity. J. Comp. Physiol. B, 159, 583–588 (1989)
Namboodiri, M.A.A.; Brownstein, M.J.; Weller, J.L.; Voisin, P.; Klein, D.C.: Multiple forms of arylalkylamine N-acetyltransferases in the rat pineal gland: purification of one molecular form. J. Pineal Res., 4, 235–246 (1987)
Deguchi, T.: Characteristics of serotonin-acetyl coenzyme A N-acetyltransferase in pineal gland of rat. J. Neurochem., 24, 1083–1085 (1975)
Morrissey, J.J.; Edwards, S.B.; Lovenberg, W.: Comparison of rat pineal gland and rat liver serotonin-N-acetyltransferase. Biochem. Biophys. Res. Commun., 77, 118–123 (1977)
Fleming, J.V.; Barrett, P.; Coon, S.L.; Klein, D.C.; Morgan, P.J.: Ovine arylalkylamine N-acetyltransferase in the pineal and pituitary glands: differences in function and regulation. Endocrinology, 140, 972–978 (1999)
Falcon, J.; Galarneau, K.M.; Weller, J.L.; Ron, B.; Chen, G.; Coon, S.L.; Klein, D.C.: Regulation of arylalkylamine N-acetyltransferase-2 (AANAT2, EC 2.3.1.87) in the fish pineal organ: evidence for a role of proteasomal proteolysis. Endocrinology, 142, 1804–1813 (2001)
Coon, S.L.; Del Olmo, E.; Young, W.S.; Klein, D.C.: Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-acetyltransferase (EC 2.3.1.87). J. Clin. Endocrinol. Metab., 87, 4699–4706 (2002)
Aisien, S.O.; Hellmund, C; Walter, R.D.: Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus. Parasitol. Res., 82, 369–371 (1996)
Obsil, T.; Ghirlando, R.; Klein, D.C.; Ganguly, S.; Dyda, F.: Crystal structure of the 14-3-3ζ:serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation. Cell, 105, 257–267 (2001)
Hamada, T.; Ootomi, M.; Horikawa, K.; Niki, T.; Wakamatu, H.; Ishida, N.: The expression of the melatonin synthesis enzyme: arylalkylamine N-acetyltransferase in the suprachiasmatic nucleus of rat brain. Biochem. Biophys. Res. Commun., 258, 772–777 (1999)
Amherd, R.; Hintermann, E.; Walz, D.; Affolter, M.; Meyer, U.A.: Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster. DNA Cell Biol., 19, 697–705 (2000)
Alonso-Gomez, A.L.; Valenciano, A.I.; Alonso-Bedate, M.; Delgado, M.J.: Differential characteristics and regulation of arylamine and arylalkylamine N-acetyltransferases in the frog retina (Rana perezi). Neurochem. Int., 26, 223–231 (1995)
Ivanova, T.N.; Michael Iuvone, P.: Melatonin synthesis in retina: circadian regulation of arylalkylamine N-acetyltransferase activity in cultured photoreceptor cells of embryonic chicken retina. Brain Res., 973, 56–63 (2003)
De Angelis, J.; Gastel, J.; Klein, D.C.; Cole, P.A.: Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87). J. Biol. Chem., 273, 3045–3050 (1998)
Tsuboi, S.; Kotani, Y.; Ogawa, K.i.; Hatanaka, T.; Yatsushiro, S.; Otsuka, M.; Moriyama, Y.: An intramolecular disulfide bridge as a catalytic switch for serotonin N-acetyltransferase. J. Biol. Chem., 277, 44229–44235 (2002)
Scheibner, K.A.; De Angelis, J.; Burley, S.K.; Cole, P.A.: Investigation of the roles of catalytic residues in serotonin N-acetyltransferase. J. Biol. Chem., 277, 18118–18126 (2002)
Khalil, E.M.; De Angelis, J.; Cole, P.A.: Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase. J. Biol. Chem., 273, 30321–30327 (1998)
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.; Fauchere, J.L.; Boutin, J.A.: Substrate specificity and inhibition studies of human serotonin N-acetyltransferase. J. Biol. Chem., 275, 8794–8805 (2000)
Ichihara, N.; Okada, M.; Takeda, M.: Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana. Insect Biochem. Mol. Biol., 32, 15–22 (2001)
Ichihara, N.; Okada, M.; Nakagawa, H.; Takeda, M.: Purification and characterization of arylalkylamine N-acetyltransferase from cockroach testicular organs. Insect Biochem. Mol. Biol., 27, 241–246 (1997)
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(2006). Aralkylamine N-acetyltransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 30. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37717-4_28
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DOI: https://doi.org/10.1007/3-540-37717-4_28
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