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. 1993 May 1;291(Pt 3):733–737. doi: 10.1042/bj2910733

Biogenic-amine acetylation: an additional function of the N-acetyltransferase from Fasciola hepatica.

S O Aisien 1, R D Walter 1
PMCID: PMC1132430  PMID: 8489501

Abstract

The previously described polyamine N-acetyltransferase from Fasciola hepatica has been observed to have an additional function, the acetylation of biogenic amines. The activities for biogenic amines, diamines and polyamines were in a constant ratio throughout the purification process. Biogenic amines found to be substrates for the enzyme included tyramine, tryptamine, beta-phenylethylamine and histamine, with Km values of 0.12 mM, 0.26 mM, 0.30 mM and 0.76 mM respectively. Octopamine, 5-hydroxytryptamine and alpha-phenylethylamine were also acceptable as substrates, though to a lesser degree. The optimum pH for biogenic-amine acetylation was 7.5, and CoA was inhibitory to the process, with a Ki of 5.5 microM. N-Acetylation appears to play a major role in the amine metabolism of this trematode. We presume that acetylation represents the process by which the parasite inactivates excess amines.

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Selected References

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  1. Aisien S. O., Walter R. D. Polyamine N-acetyltransferase from Fasciola hepatica. Mol Biochem Parasitol. 1992 Mar;51(1):65–72. doi: 10.1016/0166-6851(92)90201-t. [DOI] [PubMed] [Google Scholar]
  2. Andres H. H., Kolb H. J., Schreiber R. J., Weiss L. Characterization of the active site, substrate specificity and kinetic properties of acetyl-CoA:arylamine N-acetyltransferase from pigeon liver. Biochim Biophys Acta. 1983 Aug 16;746(3):193–201. doi: 10.1016/0167-4838(83)90074-2. [DOI] [PubMed] [Google Scholar]
  3. Blankenship J., Walle T. Acetylation of spermidine and spermine by rat liver and kidney chromatin. Arch Biochem Biophys. 1977 Feb;179(1):235–242. doi: 10.1016/0003-9861(77)90108-4. [DOI] [PubMed] [Google Scholar]
  4. Bolkenius F. N., Seiler N. Acetylderivatives as intermediates in polyamine catabolism. Int J Biochem. 1981;13(3):287–292. doi: 10.1016/0020-711x(81)90080-x. [DOI] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  6. Della Ragione F., Pegg A. E. Studies of the specificity and kinetics of rat liver spermidine/spermine N1-acetyltransferase. Biochem J. 1983 Sep 1;213(3):701–706. doi: 10.1042/bj2130701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Isaac R. E., Eaves L., Muimo R., Lamango N. N-acetylation of biogenic amines in Ascaridia galli. Parasitology. 1991 Jun;102(Pt 3):445–450. doi: 10.1017/s0031182000064428. [DOI] [PubMed] [Google Scholar]
  8. Isaac R. E., Muimo R., MacGregor A. N. N-acetylation of serotonin, octopamine and dopamine by adult Brugia pahangi. Mol Biochem Parasitol. 1990 Dec;43(2):193–198. doi: 10.1016/0166-6851(90)90144-b. [DOI] [PubMed] [Google Scholar]
  9. Libby P. R. Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities. J Biol Chem. 1978 Jan 10;253(1):233–237. [PubMed] [Google Scholar]
  10. Müller S., Walter R. D. Purification and characterization of polyamine oxidase from Ascaris suum. Biochem J. 1992 Apr 1;283(Pt 1):75–80. doi: 10.1042/bj2830075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pegg A. E., Matsui I., Seely J. E., Pritchard M. L., Pösö H. Formation of putrescine in rat liver. Med Biol. 1981 Dec;59(5-6):327–333. [PubMed] [Google Scholar]
  12. Seiler N., Bolkenius F. N., Knödgen B., Haegele K. The determination of N1-acetylspermine in mouse liver. Biochim Biophys Acta. 1981 Aug 5;676(1):1–7. doi: 10.1016/0304-4165(81)90002-7. [DOI] [PubMed] [Google Scholar]
  13. Seiler N., Bolkenius F. N., Rennert O. M. Interconversion, catabolism and elimination of the polyamines. Med Biol. 1981 Dec;59(5-6):334–346. [PubMed] [Google Scholar]
  14. Seiler N. Functions of polyamine acetylation. Can J Physiol Pharmacol. 1987 Oct;65(10):2024–2035. doi: 10.1139/y87-317. [DOI] [PubMed] [Google Scholar]
  15. Shinki T., Suda T. Purification and characterization of spermidine N1-acetyltransferase from chick duodenum. Eur J Biochem. 1989 Aug 1;183(2):285–290. doi: 10.1111/j.1432-1033.1989.tb14926.x. [DOI] [PubMed] [Google Scholar]
  16. WEISSBACH H., REDFIELD B. G., AXELROD J. The exzymic acetylation of serotonin and other naturally occurring amines. Biochim Biophys Acta. 1961 Nov 25;54:190–192. doi: 10.1016/0006-3002(61)90954-4. [DOI] [PubMed] [Google Scholar]
  17. Wittich R. M., Kilian H. D., Walter R. D. Polyamine metabolism in filarial worms. Mol Biochem Parasitol. 1987 Jun;24(2):155–162. doi: 10.1016/0166-6851(87)90102-2. [DOI] [PubMed] [Google Scholar]
  18. Wittich R. M., Walter R. D. A novel type of putrescine (diamine)-acetylating enzyme from the nematode Ascaris suum. Biochem J. 1989 May 15;260(1):265–269. doi: 10.1042/bj2600265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wittich R. M., Walter R. D. Putrescine N-acetyltransferase in Onchocerca volvulus and Ascaris suum, an enzyme which is involved in polyamine degradation and release of N-acetylputrescine. Mol Biochem Parasitol. 1990 Jan 1;38(1):13–17. doi: 10.1016/0166-6851(90)90199-v. [DOI] [PubMed] [Google Scholar]

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