This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis|
Some taxa known to possess this pathway include : Arabidopsis thaliana col, Archaea, Aves, Bacillus subtilis, Bos taurus, Geobacillus stearothermophilus, Homo sapiens, Mammalia, Physarum polycephalum, Pseudomonas aeruginosa, Saccharomyces cerevisiae, Salmonella enterica enterica serovar Typhimurium, Sulfolobus solfataricus, Teleostei
The polyamines (the most common of which are putrescine, spermidine, and spermine) are a group of positively charged organic polycations that are involved in many biological processes, including binding to nucleic acids, stabilizing membranes, and stimulating several enzymes [Tabor85, Abraham68, Frydman92, Huang90a]. While it is clear that polyamines are essential for normal cell growth, we still do not fully understand their specific molecular functions in vivo [Tabor85]. putrescine and spermidine are found in all life forms, and spermine is found mostly in eukaryotes. A few bacterial species that were reported to contain spermine include Pseudomonas aeruginosa [Stevens68] and Geobacillus stearothermophilus [Weaver58].
Unlike spermidine, spermine is not essential for viability in eukaryotes. Exogenous spermine supported growth of spermidine-depleted cells only after its degradation into spermidine [Kramer96] and spermine-defficient transgenic mice, which were generated by eliminating the SpmS gene, located on the X chromosome, were viable [Lorenz98]. Although, the lack of spermine biosynthesis resulted in a phenotype in affected males that included symptoms of circling behavior, hyperactivity, head shaking, inner ear abnormalities, deafness, sterility, a profound postnatal growth retardation, and a propensity to sudden death. The symptoms were eliminated when the gene was overexpressed in the mice. These results showed that spermine synthesis is needed for normal growth, viability, and fertility in male mice [Wang04b].
In Saccharomyces cerevisiae the lack of SPE4 had no obvious manifestation on the mutant phenotype and the homozygous Δspe4 diploid cells sporulated normally indicating that spermine in yeast was not essential for growth and development. Hence, the role of spermine in yeast remains unclear and needs further research. The high amino acid identity (50%) between the spermidine synthase and spermine synthase prompted the suggestion that spermine synthase may have been descended from spermidine synthase by gene duplication [HamasakiKatagir98].
spermine is formed by the addition of a propylamine moiety to spermidine, catalyzed by an aminopropyltransferase termed spermine synthase. The source of the propylamine group is decarboxylated S-adenosyl-L-methionine ( S-adenosyl 3-(methylthio)propylamine) which is produced by the action of the pyruvoyl-containing enzyme S-adenosylmethionine decarboxylase. The other product of the aminopropyltransferase reaction is S-methyl-5'-thioadenosine (MTA), which is recycled back to L-methionine.
Unification Links: AraCyc:ARGSPECAT-PWY
Hartmut Foerster on Wed Mar 30, 2005:
renamed spermine biosynthesis to spermine biosynthesis I, because there were two pathways called spermine biosynthesis
Abraham68: Abraham KA (1968). "Studies on DNA-dependent RNA polymerase from Escherichia coli. 1. The mechanism of polyamine induced stimulation of enzyme activity." Eur J Biochem 5(1);143-6. PMID: 4873311
Frydman92: Frydman L, Rossomando PC, Frydman V, Fernandez CO, Frydman B, Samejima K (1992). "Interactions between natural polyamines and tRNA: an 15N NMR analysis." Proc Natl Acad Sci U S A 89(19);9186-90. PMID: 1409623
HamasakiKatagir98: Hamasaki-Katagiri N, Katagiri Y, Tabor CW, Tabor H (1998). "Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant." Gene 210(2);195-201. PMID: 9573363
Huang90a: Huang SC, Panagiotidis CA, Canellakis ES (1990). "Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli." Proc Natl Acad Sci U S A 87(9);3464-8. PMID: 2185470
Lorenz98: Lorenz B, Francis F, Gempel K, Boddrich A, Josten M, Schmahl W, Schmidt J, Lehrach H, Meitinger T, Strom TM (1998). "Spermine deficiency in Gy mice caused by deletion of the spermine synthase gene." Hum Mol Genet 7(3);541-7. PMID: 9467015
Wang04b: Wang X, Ikeguchi Y, McCloskey DE, Nelson P, Pegg AE (2004). "Spermine synthesis is required for normal viability, growth, and fertility in the mouse." J Biol Chem 279(49);51370-5. PMID: 15459188
Balasundaram94: Balasundaram D, Xie QW, Tabor CW, Tabor H (1994). "The presence of an active S-adenosylmethionine decarboxylase gene increases the growth defect observed in Saccharomyces cerevisiae mutants unable to synthesize putrescine, spermidine, and spermine." J Bacteriol 176(20);6407-9. PMID: 7929015
Diaz91: Diaz E, Anton DL (1991). "Alkylation of an active-site cysteinyl residue during substrate-dependent inactivation of Escherichia coli S-adenosylmethionine decarboxylase." Biochemistry 1991;30(16);4078-81. PMID: 2018773
Ekstrom99: Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE (1999). "The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold." Structure Fold Des 7(5);583-95. PMID: 10378277
Kashiwagi90: Kashiwagi K, Taneja SK, Liu TY, Tabor CW, Tabor H (1990). "Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase." J Biol Chem 265(36);22321-8. PMID: 2266128
Korhonen95: Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J (1995). "Molecular cloning of a cDNA encoding human spermine synthase." DNA Cell Biol 14(10);841-7. PMID: 7546290
Li01: Li YF, Hess S, Pannell LK, White Tabor C, Tabor H (2001). "In vivo mechanism-based inactivation of S-adenosylmethionine decarboxylases from Escherichia coli, Salmonella typhimurium, and Saccharomyces cerevisiae." Proc Natl Acad Sci U S A 98(19);10578-83. PMID: 11526206
Markham82: Markham GD, Tabor CW, Tabor H (1982). "S-adenosylmethionine decarboxylase of Escherichia coli. Studies on the covalently linked pyruvate required for activity." J Biol Chem 257(20);12063-8. PMID: 6749853
Pajunen88: Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE (1988). "Structure and regulation of mammalian S-adenosylmethionine decarboxylase." J Biol Chem 263(32);17040-9. PMID: 2460457
Pegg86: Pegg AE, Coward JK, Talekar RR, Secrist JA (1986). "Effects of certain 5'-substituted adenosines on polyamine synthesis: selective inhibitors of spermine synthase." Biochemistry 1986;25(14);4091-7. PMID: 3091070
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