[1. Boyer, P. D., Lardy, H., & Myrback, K. (1963). The enzymes (Vol. 8, pp. 337-351). New York: Academic Press.]Search in Google Scholar
[2. Miller, J. R., & Edmondson, D. E. (1999). Structure- -activity relationships in the oxidation of para- -substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry, 38, 13670-13682.10.1021/bi990920y]Search in Google Scholar
[3. Silverman, R. B., Hoffman, S. J., & Catus III, W. B. (1980). A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation. J. Am. Chem. Soc., 102, 7126-7128.10.1021/ja00543a052]Search in Google Scholar
[4. Tsugeno, Y., & Ito, A. (1997). A key amino acid responsible for substrate selectivity of monoamine oxidase A and B. J. Biol. Chem., 272, 14033-14036.10.1074/jbc.272.22.14033]Search in Google Scholar
[5. Yu, P. H. (1988). Three types of stereospecifi city and the kinetic deuterium isotope effects in the oxidative deamination of dopamine as catalyzed by different amine oxidases. Biochem. Cell Biol., 66, 853-861.10.1139/o88-097]Search in Google Scholar
[6. Yu, P. H., Bailey, B. A., Durden, D. A., & Boulton A. A. (1986). Stereospecifi c deuterium substitution at the α-carbon position of dopamine and its effect on oxidative deamination catalyzed by MAO-A and MAO-B from different tissues. Biochem. Pharmacol., 35, 1027-1036.10.1016/0006-2952(86)90094-8]Search in Google Scholar
[7. Yu, P. H., Kazakoff, C., Davis, B. A., & Boulton, A. A. (1982). Deuterium isotope effect on the enzymatic oxidation of dopamine and serotonin. Biochem. Pharmacol., 31, 3697-3698.10.1016/0006-2952(82)90601-3]Search in Google Scholar
[8. Kalgutkar, A. S., Deepak, K., Dalvie, D. K., Castagnoli, N. Jr., & Taylor, T. J. (2001). Interactions of nitrogen- -containing xenobitics with monoamine oxidase (MAO) isozymes A and B: SAR studies on MAO substrates and inhibitors. Chem. Res. Toxicol., 14, 1139-1162.10.1021/tx010073b]Search in Google Scholar
[9. Kema, I. P., De Vries, E. G. E., & Muskiet, F. A. J. (2000). Clinical chemistry of serotonin and metabolites. J. Chromatogr. B, 747, 33-48.10.1016/S0378-4347(00)00341-8]Search in Google Scholar
[10. Semak, I., Korik, E., Naumova, M., Wortsman, J., & Slominski, A. (2004). Serotonin metabolism in rat skin: characterization by liquid chromatography-mass spectrometry. Arch. Biochem. Biophys., 421, 61-66.10.1016/j.abb.2003.08.03614678785]Search in Google Scholar
[11. Kang, S., Kang, K., Lee, K., & Back, K. (2007). Characterization of tryptamine 5-hydroxylase and serotonin synthesis in rice plants. Plant Cell Reports, 26, 2009-2015.10.1007/s00299-007-0405-917639402]Search in Google Scholar
[12. Komissarov, I. V., Abraments, I. I., & Samoilovich, I. M. (1989). Tryptamine as an endogenous modulator of neuronal sensitivity to serotonin. Neurophysiology, 21, 254-258.10.1007/BF01058225]Search in Google Scholar
[13. Jacob, M. S., & Presti, D. E. (2005). Endogenous psychoactive tryptamines reconsidered: an anxiolytic role for dimethyltryptamine. Med. Hypotheses, 64, 930-937.10.1016/j.mehy.2004.11.005]Search in Google Scholar
[14. Hocck, D. R., & Floss, H. G. (1981). Preparation of stereospecifi cally α- and β-tritiated tryptamine and the stereochemistry of aromatic L-amino acid decarboxylase. J. Nat. Prod., 44, 759-762.10.1021/np50018a031]Search in Google Scholar
[15. Bomanji, J. B., Costa, D. C., & Ell, P. J. (2001). Clinical role of positron emission tomography in oncology. Lancet Oncol., 2, 157-64.10.1016/S1470-2045(00)00257-6]Search in Google Scholar
[16. Pacak, K., Eisenhofer, G., Carrasquillo, J. A., Chen, C. C, Li, Sheng-Ting, & Goldstein, D. S. (2001), 6-[18F] Fluorodopamine Positron Emission Tomographic (PET) scanning for diagnostic localization of pheochromocytoma. Hypertension, 38, 6-8.10.1161/01.HYP.38.1.611463751]Search in Google Scholar
[17. Huskey, W. P. (1991). Origins and interpretations of heavy-atom isotope effects. In P. F. Cook (Ed.) Enzyme mechanism from isotope effects (pp. 37-73). Boca Raton: CRC Press.]Search in Google Scholar
[18. Schowen, R. I. (1972). Mechanistic deductions from solvent isotope effects. Prog. Phys. Org. Chem., 9, 275-329.10.1002/9780470171882.ch6]Search in Google Scholar
[19. Dragulska, S., & Kańska, M. (2014). Enzymatic synthesis of tryptamine and its halogen derivatives selectively labeled with hydrogen isotopes. J. Radioanal. Nucl. Chem., 299, 759-763.10.1007/s10967-013-2816-0451460726224955]Search in Google Scholar
[20. Ivanović, I. D., & Majkić-Singh, N. (1988). Determination of platelet monoamine oxidase by new continuous spectrophotometric method. J. Clin. Chem. Clin. Biochem., 26, 447-451.10.1515/cclm.1988.26.7.4473221175]Search in Google Scholar
[21. Wigley, L. J., Mantle, P. G., & Perry, D. A. (2006). Natural and directed biosynthesis of communes in alkaloids. Phytochemistry, 67, 561-569.10.1016/j.phytochem.2005.10.01116324729]Search in Google Scholar
[22. Gary, R., Bates, R. G., & Robinson, R. A. (1964). Second dissociation constant of deuterio phosphoric acid in deuterium oxide from 5 to 50°C: Standardization of pD scale. J. Phys. Chem., 68, 3806-3809.10.1021/j100794a046]Search in Google Scholar
[23. Parkin, D. W. (1991). Methods for determination of competitive and noncompetitive Kinetic Isotope Effects. In P. F. Cook (Ed.) Enzyme mechanism from isotope effects (pp. 269-290). Boca Raton: CRC Press.]Search in Google Scholar
[24. Kadnikova, E. N., & Kostić N. M. (2002). Oxidation of ABTS by hydrogen peroxide catalyzed by horseradish peroxidase encapsulated into sol-gel glass. Effects of glass matrix on reactivity. J. Mol. Catal. B-Enzym., 18, 39-48.10.1016/S1381-1177(02)00057-7]Search in Google Scholar
[25. Pałka, K., Szymańska, J., & Kańska, M. (2012). The kinetic and solvent deuterium isotope effects in oxidation of putrescine catalyzed by enzyme diamine oxidase. Isot. Environ. Health Stud., 49, 3-8.10.1080/10256016.2012.68352522540261]Search in Google Scholar
[26. Papajak, E., Kwiecień, R. A., Rudziński, J., Sicińska, D., Kamiński, R., Szatkowski, Ł., Kurihara, T., Esaki, N., & Paneth, P. (2006). Mechanism of the reaction catalyzed by DL-2-haloacid dehalogenase as determined from Kinetic Isotope Effects. Biochemistry, 45, 6012-6017.10.1021/bi051955316681373]Search in Google Scholar
[27. Northrop, D. B. (1975). Steady-state analysis of kinetic isotope effects in enzymatic reactions. Biochemistry, 14, 2644-2650. 10.1021/bi00683a0131148173]Search in Google Scholar