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. 1981 Aug 1;197(2):315–320. doi: 10.1042/bj1970315

Specificity of mammalian spermidine synthase and spermine synthase.

A E Pegg, K Shuttleworth, H Hibasami
PMCID: PMC1163129  PMID: 6798961

Abstract

1. The specificity of rat prostatic spermidine synthase and spermine synthase with respect to the amine acceptor of the propylamine group was studied. 2. Spermidine synthase could use cadaverine (1,5-diaminopentane) instead of putrescine, but the Km for cadaverine was much greater and the rate with 1mM-cadaverine was only 10% of that with putrescine. 1,3-Diaminopropane was even less active (2% of the rate with putrescine) and no other compound tested (including longer alpha,omega-diamines, spermidine and its homologues and monoacetyl derivatives) was active. 3. Spermine synthase was equally specific. The only compounds tested that showed any activity were 1,8-diamino-octane, sym-homospermidine, sym-norspermidine and N-(3-aminopropyl)-cadaverine, which at 1mM gave rates 2, 17, 3 and 4% of the rate with spermidine respectively. 4. The formation of polyamine derivatives of cadaverine and to a very small extent of 1,3-diaminopropane was confirmed by exposing transformed mouse fibroblasts to these diamines when synthesis of putrescine was prevented by alpha-difluoromethylornithine. Under these conditions the cells accumulated significant amounts of N-(3-aminopropyl)cadaverine and NN'-bis(3-aminopropyl)cadaverine when exposed to cadaverine and small amounts of sym-norspermidine and sym-norspermine when exposed to 1,3-diaminopropane.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aleksijevic A., Grove J., Schuber F. Studies on polyamine biosynthesis in Euglena gracilis. Biochim Biophys Acta. 1979 Nov 22;565(1):199–207. doi: 10.1016/0005-2787(79)90096-0. [DOI] [PubMed] [Google Scholar]
  2. Alhonen-Hongisto L., Jänne J. Polyamine depletion induces enhanced synthesis and accumulation of cadaverine in cultured Ehrlich ascites carcinoma cells. Biochem Biophys Res Commun. 1980 Apr 29;93(4):1005–1013. doi: 10.1016/0006-291x(80)90589-6. [DOI] [PubMed] [Google Scholar]
  3. Alhonen-Hongisto L., Pösö H., Jänne J. Inhibition of polyamine accumulation and cell proliferation by derivatives of diaminopropane in Ehrlich ascites cells grown in culture. Biochim Biophys Acta. 1979 Oct 25;564(3):473–487. doi: 10.1016/0005-2787(79)90037-6. [DOI] [PubMed] [Google Scholar]
  4. Bethell D. R., Pegg A. E. Effects of diamines on ornithine decarboxylase activity in control and virally transformed mouse fibroblasts. Biochem J. 1979 Apr 15;180(1):87–94. doi: 10.1042/bj1800087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bowman W. H., Tabor C. W., Tabor H. Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J Biol Chem. 1973 Apr 10;248(7):2480–2486. [PubMed] [Google Scholar]
  6. Coward J. K., Motola N. C., Moyer J. D. Polyamine biosynthesis in rat prostate. Substrate and inhibitor properties of 7-deaza analogues of decarboxylated S-adenosylmethionine and 5'-methylthioadenosine. J Med Chem. 1977 Apr;20(4):500–505. doi: 10.1021/jm00214a008. [DOI] [PubMed] [Google Scholar]
  7. Dion A. S., Cohen S. S. Polyamines in the synthesis of bacteriophage deoxyribonucleic acid. II. Requirement for polyamines in T4 infection of a polyamine auxotroph. J Virol. 1972 Mar;9(3):423–430. doi: 10.1128/jvi.9.3.423-430.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hamana K., Matsuzaki S. Occurrence of sym-homospermidine in the Japanese newt, Cynops pyrrhogaster pyrrhogaster. FEBS Lett. 1979 Mar 15;99(2):325–328. doi: 10.1016/0014-5793(79)80983-7. [DOI] [PubMed] [Google Scholar]
  9. Hannonen P., Jänne J., Raina A. Separation and partial purification of S-adenosylmethionine decarboxylase and spermidine and spermine synthases from rat liver. Biochem Biophys Res Commun. 1972 Jan 31;46(2):341–348. doi: 10.1016/s0006-291x(72)80144-x. [DOI] [PubMed] [Google Scholar]
  10. Henningsson S., Persson L., Rosengren E. Biosynthesis of cadaverine in mice under the influence of an anabolic steroid. Acta Physiol Scand. 1976 Dec;98(4):445–449. doi: 10.1111/j.1748-1716.1976.tb10334.x. [DOI] [PubMed] [Google Scholar]
  11. Hibasami H., Borchardt R. T., Chen S. Y., Coward J. K., Pegg A. E. Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem J. 1980 May 1;187(2):419–428. doi: 10.1042/bj1870419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hibasami H., Pegg A. E. Differential inhibition of mammalian aminopropyltransferase activities. Biochem Biophys Res Commun. 1978 Apr 28;81(4):1398–1405. doi: 10.1016/0006-291x(78)91291-3. [DOI] [PubMed] [Google Scholar]
  13. Hibasami H., Pegg A. E. Rapid and convenient method for the assay of aminopropyltransferases. Biochem J. 1978 Mar 1;169(3):709–712. doi: 10.1042/bj1690709. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hölttä E., Jänne J., Hovi T. Suppression of the formation of polyamines and macromolecules by DL-alpha-difluoromethylornithine and methylglyoxal bis(guanylhydrazone) in phytohaemagglutinin-activated human lymphocytes. Biochem J. 1979 Jan 15;178(1):109–117. doi: 10.1042/bj1780109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jänne J., Pösö H., Raina A. Polyamines in rapid growth and cancer. Biochim Biophys Acta. 1978 Apr 6;473(3-4):241–293. doi: 10.1016/0304-419x(78)90015-x. [DOI] [PubMed] [Google Scholar]
  16. Jänne J., Williams-Ashman H. G. Dissociation of putrescine-activated decarboxylation of S-adenosyl-L-methionine from the enzymic synthesis of spermidine and spermine by purified prostatic enzyme preparations. Biochem Biophys Res Commun. 1971 Jan 22;42(2):222–229. [PubMed] [Google Scholar]
  17. Kallio A., Pösö H., Guha S. K., Jänne J. Polyamines and their biosynthetic enzymes in Ehrlich ascites-carcinoma cells. Modification of tumour polyamine pattern by diamines. Biochem J. 1977 Jul 15;166(1):89–94. doi: 10.1042/bj1660089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pajula R. L., Raina A., Eloranta T. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain. Eur J Biochem. 1979 Nov;101(2):619–626. doi: 10.1111/j.1432-1033.1979.tb19756.x. [DOI] [PubMed] [Google Scholar]
  19. Pajula R. L., Raina A. Methylthioadenosine, a potent inhibitor of spermine synthase from bovine brain. FEBS Lett. 1979 Mar 15;99(2):343–345. doi: 10.1016/0014-5793(79)80988-6. [DOI] [PubMed] [Google Scholar]
  20. Pegg A. E., Borchardt R. T., Coward J. K. Effects of inhibitors of spermidine and spermine synthesis on polyamine concentrations and growth of transformed mouse fibroblasts. Biochem J. 1981 Jan 15;194(1):79–89. doi: 10.1042/bj1940079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pegg A. E., McGill S. Decarboxylation of ornithine and lysine in rat tissues. Biochim Biophys Acta. 1979 Jun 6;568(2):416–427. doi: 10.1016/0005-2744(79)90310-3. [DOI] [PubMed] [Google Scholar]
  22. Persson L. Evidence of decarboxylation of lysine by mammalian ornithine decarboxylase. Acta Physiol Scand. 1977 Aug;100(4):424–429. doi: 10.1111/j.1748-1716.1977.tb05966.x. [DOI] [PubMed] [Google Scholar]
  23. Samejima K., Nakazawa Y. Action of decarboxylated S-adenosylmethionine analogs in the spermidine-synthesizing system from rat prostate. Arch Biochem Biophys. 1980 Apr 15;201(1):241–246. doi: 10.1016/0003-9861(80)90508-1. [DOI] [PubMed] [Google Scholar]
  24. Seidenfeld J., Marton L. J. Depletion of intracellular putrescine and spermidine by alpha-difluromethylornithine does not inhibit proliferation of 9L rat brain tumor cells. Biochem Biophys Res Commun. 1979 Feb 28;86(4):1192–1198. doi: 10.1016/0006-291x(79)90243-2. [DOI] [PubMed] [Google Scholar]
  25. Srivenugopal K. S., Adiga P. R. Enzymic synthesis of sym-homospermidine in Lathyrus sativus (grass pea) seedlings. Biochem J. 1980 Aug 15;190(2):461–464. doi: 10.1042/bj1900461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tabor C. W., Tabor H. 1,4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem. 1976;45:285–306. doi: 10.1146/annurev.bi.45.070176.001441. [DOI] [PubMed] [Google Scholar]
  27. Tait G. H. The formation of homospermidine by an enzyme from Rhodopseudomonas viridis [proceedings]. Biochem Soc Trans. 1979 Feb;7(1):199–201. doi: 10.1042/bst0070199. [DOI] [PubMed] [Google Scholar]
  28. Tang K. C., Pegg A. E., Coward J. K. Specific and potent inhibition of spermidine synthase by the transition-state analog, S-adenosyl-3-thio-1,8-diaminooctane. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1371–1377. doi: 10.1016/0006-291x(80)90102-3. [DOI] [PubMed] [Google Scholar]
  29. Zappia V., Cacciapuoti G., Pontoni G., Oliva A. Mechanism of propylamine-transfer reactions. Kinetic and inhibition studies on spermidine synthase from Escherichia coli. J Biol Chem. 1980 Aug 10;255(15):7276–7280. [PubMed] [Google Scholar]

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