Abstract
S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine. Its product, decarboxylated S-adenosylmethionine (dcAdoMet) is used as an aminopropyl donor by spermidine synthase and spermine synthase (Williams-Ashman and Pegg, 1981; Pegg and McCann, 1982; Tabor and Tabor, 1984a). Once decarboxylated by the action of AdoMetDC, S-adenosylmethionine (AdoMet) becomes committed to polyamine production since methyltransferases use dcAdoMet very poorly, if at all (Pegg, 1984, 1986). In fact, the only known metabolic route for further metabolism of dcAdoMet apart for its use as an aminopropyltransferase substrate is its acetylation (Wagner et al., 1985; Pegg et al., 1986) The supply of dcAdoMet is normally regulated very tightly by the cellular polyamine content and this regulation is brought about by changes in the activity of AdoMetDC (Pegg, 1984). In this way, the cellular content of dcAdoMet is usually kept very low (about 1–3% of AdoMet content) as its synthesis is linked to the ability of the aminopropyltransferases to use it to form polyamines. Only when cellular polyamine metabolism is deranged by inhibition of the other enzymes in the polyamine biosynthetic pathway does the dcAdoMet content rise. Increases of several hundred fold occur when ornithine decarboxylase (ODC) activity is inhibited by drugs such as α-difluoromethylornithine (DFMO) and, only under these conditions, is the acetyl derivative of dcAdoMet formed in significant amounts (Pegg, 1986). The increased content of dcAdoMet is due to both an increase in the activity of AdoMetDC (Alhonen-Hongisto, 1980; Mamont et al., 1981; Pegg, 1984) and to the inability of the aminopropyltransferases to utilize the dcAdoMet formed by it because of the absence of putrescine and spermidine to serve as aminopropyl acceptors.
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References
Alhonen-Hongisto, L., 1980, Regulation of S-adenosylmethionine decarboxylase by polyamines in Ehrlich ascites-carcinoma cells grown in culture, Biochem. J., 190: 747.
Artamonova, E. Y., Zavalova, L. L., Khomutov, R. M., and Khomutov, A. R., 1986, Irreversible inhibition of S-adenosylmethionine decarboxylase by hydroxylamine-containing analogues of decarboxylated S-adenosylmethionine, Biorg. Khim., 12: 206.
Dowhan, L., and Li, Q., 1988, Formation of the pyruvate residue of phosphatidylserine decarboxylase of E. coli, FASEB J., 46: Abst. 2349.
Hickok, N. J., Seppänen, P. J., Kontula, K. K., Jänne, P. A., Bardin, C. W., and Jänne, O. A., 1986, Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3′ termini, Proc. Natl. Acad. Sci. USA, 83: 594.
Huynh, Q. K., and Snell, E., 1986, Histidine decarboxylase from Lactobacillus 30a. Hydroxylamine clevages of the-seryl-seryl-bond at the activation site of prohistidine decarboxylase, J. Biol. Chem., 261: 1521.
Kameji, T., and Pegg, A. E., 1987a, Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase, Biochem. J., 243: 285.
Kameji, T., and Pegg, A. E., 1987b, Inhibition of translation of mRNAs for ornithine decarboxylase and S-adenosylmethionine decarboxylase by polyamines, J. Biol. Chem., 262: 2427.
Kolb, M., Danzin, C., Barth, J., and Calverie, N., 1982, Synthesis and biochemical properties of chemically stable product analogues of the reaction catalyzed by S-adenosylmethionine decarboxylase, J. Med. Chem., 25: 550.
Kozak, M., 1987, At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells, J. Mol. Biol., 196: 947.
Mach, M., White, M. W., Neubauer, M., Degen, J. L., and Morris, D. R., 1986, Isolation of a cDNA clone encoding S-adenosylmethionine decarboxylase. Expression of the gene in mitogen-activated lymphocytes, J. Biol. Chem., 261: 11697.
Madhubala, R., Secrist in, J. A., and Pegg, A. E., 1988, Effect of inhibitors of S-adenosylmethionine decarboxylase on the contents of ornithine decarboxylase and S-adenosylmethionine decarboxylase in L1210 cells, Biochem. J., 254: 45.
Mamont, P., Joder-Ohlenbusch, A. M., Nussli, M., and Grove, J., 1981, Indirect evidence for a strict negative control of S-adenosylmethionine decarboxylase by spermidine in rat hepatoma cells, Biochem. J., 196: 411.
Pajunen, A., Crozat, A., Jänne, G. A., Ihalainen, R., Laitinen, P. H., Stanley, B., Madhubala, R., and Pegg, A. E., 1988, Structure and regulation of S-adenosylmethionine decarboxylase, J. Biol. Chem., in press.
Pegg, A. E., 1984, S-adenosylmethionine decarboxylase: a brief review, Cell Biochem. and function, 2: 11.
Pegg, A. E., 1986, Recent advances in the biochemistry of polyamines in eukaryotes, Biochem. J., 234: 249.
Pegg, A. E., 1988, Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy, Cancer Res., 48: 759.
Pegg, A. E., and Jacobs, G., 1983, Comparison of inhibitors of S-adenosylmethionine decarboxylase from different species, Biochem. J., 213: 495.
Pegg, A. E., and McCann, P. P., 1982, Polyamine metabolism and function, Am. J. Physiol., 243: C212.
Pegg, A. E., Wechter, R., Clark, R. S., Wiest, L., and Erwin, B. G., 1986, Acetylation of decarboxylated S-adenosylmethionine by mammalian cells, Biochemistry, 25: 379.
Pegg, A. E., Wechter, R., and Pajunen, A., 1987, Increase in S-adenosylmethionine decarboxylase activity in SV-3T3 cells treated with S-methyl-5′-methylthioadenosine, Biochem. J., 244: 49.
Pegg, A. E., Jones, D. B., and Secristhi, J. A., 1988a, Effect of inhibitors of S-adenosylmethionine decarboxylase on polyamine content and growth of L1210 cells, Biochemistry, 24: 1408.
Pegg, A. E., Wiest, L., and Pajunen, A., 1988b, Detection of proenzyme form of S-adenosylmethionine decarboxylase in extracts from rat prostate, Biochem. Biophys. Res. Commun, 150: 788.
Pegg, A. E., Kameji, T., Shirahata, A., Stanley, B., Madhubala, R., and Pajunen, A., 1988c, Regulation of mammalian S-adenosylmethionine decarboxylase, Advan. Enzyme Regul., 27: 43.
Porter, C. W., and Bergeron, R. J., 1988, Enzyme regulation as an approach to interference with polyamine biosynthesis-an alternative to enzyme inhibition, Advan. Enzyme Regul., 27: 57.
Pösö, H., and Pegg, A. E., 1981, Differences between tissues in response of S-adenosylmethionine decarboxylase to administration of polyamines, Biochem. J., 200: 629.
Pösö, H., and Pegg, A. E., 1982, Comparison of S-adenosylmethionine decarboxylases from rat liver and muscle, Biochemistry, 21: 3116.
Radford, D. M., Eddy, R., Haley, L., Henry, W. M., Pajunen, A., Pegg, A. E., and Shows, T. B., 1988, Gene sequences coding for S-adenosylmethionine decarboxylase are present on chromosomes 6 and X and are not amplified in colon neoplasia, Cytogenet. Cell Genet, submitted.
Rechsteiner, M., 1988, Regulation of enzyme levels by proteolysis: the role of PEST regions, Advan. Enzyme Regul., 27: 135.
Recsei, P., and Snell, E., 1984, Pyruvoyl enzymes, Annu. Rev. Biochem., 53: 357.
Rogers, S., Wells, S., and Rechsteiner, M., 1986, Amino acid sequences common to rapidly degraded protein: the PEST hypothesis, Science, 234: 364.
Shirahata, A., and Pegg, A. E., 1985, Regulation of S-adenosylmethionine decarboxylase activity in rat liver and prostate, J. Biol. Chem., 260: 9583.
Shirahata, A., and Pegg, A. E., 1986, Increased content of mRNA for a precursor of S-adenosylmethionine decarboxylase in rat prostate after treatment with 2-difluoromethionine, J. Biol. Chem., 261: 13833.
Shirahata, A., Christman, K., and Pegg, A. E., 1985, Quantitation of S-adenosylmethionine decarboxylase protein, Biochemistry, 24: 4417.
Tabor, C. W., and Tabor, C. H., 1984a, Polyamines, Annu. Rev. Biochem., 53: 749.
Tabor, C. W., and Tabor, H., 1984b, Methionine adenosyltransferase (S-adenosylmethionine synthetase) and S-adenosylmethionine decarboxylase, Advan. Enzymol. Related Areas Mol. Biol., 56: 251–282.
Tabor, C. W., and Tabor, H., 1987, The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase, J. Biol. Chem., 262: 16037.
Wagner, J., Hirth, Y., Piriou, R., Zakett, D., Claverie, N., and Danzin, C., 1985, N-Acetyl decarboxylated S-adenosylmethionine, a new metabolite of decarboxylated S-àdenosylmethionine: isolation and characterization, Biochem. Biophys. Res. Commun., 133: 546–553.
White, M. W., and Morris, D. R., 1988, S-adenosylmethionine decarboxylase: genes and expression, In: “The Physiology of Polyamines, ” U. Bachrach, and Y. M. Heimer, Eds., CRC Press, Boca Raton, in press.
Williams-Ashman, H. G., and Pegg, A. E., 1981, Aminopropyl group transfers, In: “Polyamines in Biology and Medicine,” D. R. Morris, and L. J. Marton, Eds., Marcel Dekker, New York, p. 407.
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Pegg, A.E., Stanley, B., Pajunen, A., Crozat, A., Jänne, O.A. (1988). Properties of Human and Rodent S-Adenosylmethionine Decarboxylase. In: Zappia, V., Pegg, A.E. (eds) Progress in Polyamine Research. Advances in Experimental Medicine and Biology, vol 250. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5637-0_10
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