2.0 2012-05-31 14:39:22 -0600 2015-06-03 17:19:47 -0600 ECMDB20325 M2MDB001159 Decarboxy-SAM dcSAM is a member of the chemical class known as Purine Nucleosides and Analogues. These are compounds comprising a purine base attached to a sugar. [2-(Amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulphonium+ ++, the amino-oxy analogue of decarboxylated S-adenosylmethionine, is a potent irreversible inhibitor of Escherichia coli S-adenosylmethionine decarboxylase [Khomutov, Zavalova, Syrku, Artamonova &amp; Khomutov (1983) Bioorg. (PMID 1872800) (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulphonium salt 3-amino-propyl-<i>S</i>-adenosine 3-Amino-propyl-S-adenosine <i>S</i>-adenosylmethioninamine <i>S</i>-methyl-<i>S</i>-adenosyl homocysteamine Dadomet DcSAM Decarboxylated adomet Decarboxylated S-adenosylmethionine Decarboxylated sam S-Adenosyl-(5')-3-methylthiopropylamine S-Adenosyl-L-methioninamine S-Adenosylmethioninamine S-Methyl-S-adenosyl homocysteamine C14H24N6O3S 356.444 356.163059354 {[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(3-azaniumylpropyl)methylsulfanium S-adenosylmethioninaminium [H][C@]1(C[S+](C)CCC[NH3+])O[C@@]([H])(N2C=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O InChI=1S/C14H23N6O3S/c1-24(4-2-3-15)5-8-10(21)11(22)14(23-8)20-7-19-9-12(16)17-6-18-13(9)20/h6-8,10-11,14,21-22H,2-5,15H2,1H3,(H2,16,17,18)/q+1/p+1/t8-,10-,11-,14-,24?/m1/s1 ZUNBITIXDCPNSD-LSRJEVITSA-O Cytoplasm Periplasm logp -1.73 ALOGPS logs -2.96 ALOGPS solubility 4.72e-01 g/l ALOGPS logp -2.8 ChemAxon pka_strongest_acidic 12.45 ChemAxon pka_strongest_basic 10.09 ChemAxon iupac {[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(3-azaniumylpropyl)methylsulfanium ChemAxon average_mass 356.444 ChemAxon mono_mass 356.163059354 ChemAxon smiles [H][C@]1(C[S+](C)CCC[NH3+])O[C@@]([H])(N2C=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O ChemAxon formula C14H24N6O3S ChemAxon inchi InChI=1S/C14H23N6O3S/c1-24(4-2-3-15)5-8-10(21)11(22)14(23-8)20-7-19-9-12(16)17-6-18-13(9)20/h6-8,10-11,14,21-22H,2-5,15H2,1H3,(H2,16,17,18)/q+1/p+1/t8-,10-,11-,14-,24?/m1/s1 ChemAxon inchikey ZUNBITIXDCPNSD-LSRJEVITSA-O ChemAxon polar_surface_area 146.95 ChemAxon refractivity 101.7 ChemAxon polarizability 37.34 ChemAxon rotatable_bond_count 6 ChemAxon acceptor_count 7 ChemAxon donor_count 4 ChemAxon physiological_charge 2 ChemAxon formal_charge 2 ChemAxon Spermidine Biosynthesis I Spermidine is formed by the addition of a propylamine moiety to putrescine, catalyzed by an aminopropyltransferase termed spermidine synthase, the the product of gene speE. The source of the propylamine group is decarboxylated S-adenosyl-L-methionine (S-adenosyl-L-methioninamine) which is produced by the action of the pyruvoyl-containing enzyme adenosylmethionine decarboxylase. The other product of the aminopropyltransferase reaction is S-methyl-5'-thioadenosine (MTA), which can be recycled back to L-methionine in many organisms, but not in E. coli. Inhibition of E. coli adenosylmethionine decarboxylase by spermidine appears to be the most significant regulator of polyamine biosynthesis, probably limiting it when the intracellular spermidine concentration becomes excessive. In E. coli most intracellular spermidine is bound to nucleic acids and phospholipids. (EcoCyc) PW002040 Metabolic aminopropylcadaverine biosynthesis Polyamines are important for cell growth and are believed to be involved in many processes including DNA, RNA, and protein synthesis, as well as membrane integrity and resistance to stress, to name a few. Cadaverine and aminopropylcadaverine are alternative polyamines that can at least partially substitute for purtrescine and spermidine, the primary polyamines found in E. coli. Lysine is decarboxylated to form cadaverine which is then converted to aminopropylcadaverine by the aminopropyltransferase, SpeE. (EcoCyc) PW002039 Metabolic aminopropylcadaverine biosynthesis PWY0-1303 spermidine biosynthesis I BSUBPOLYAMSYN-PWY Specdb::NmrOneD 264788 Specdb::NmrOneD 264789 Specdb::NmrOneD 264790 Specdb::NmrOneD 264791 Specdb::NmrOneD 264792 Specdb::NmrOneD 264793 Specdb::NmrOneD 264794 Specdb::NmrOneD 264795 Specdb::NmrOneD 264796 Specdb::NmrOneD 264797 Specdb::NmrOneD 264798 Specdb::NmrOneD 264799 Specdb::NmrOneD 264800 Specdb::NmrOneD 264801 Specdb::NmrOneD 264802 Specdb::NmrOneD 264803 Specdb::NmrOneD 264804 Specdb::NmrOneD 264805 Specdb::NmrOneD 264806 Specdb::NmrOneD 264807 25203490 26330790 S-ADENOSYLMETHIONINAMINE Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. 21097882 Weitkamp, E. L., Dixon, H. B., Khomutov, A. R., Khomutov, R. M. (1991). "Effect of magnesium ions on the inhibition of S-adenosylmethionine decarboxylase from Escherichia coli by [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulphonium ." Biochem J 277 ( Pt 3):643-645. 1872800 Spermidine synthase P09158 SPEE_ECOLI speE http://ecmdb.ca/proteins/P09158.xml S-adenosylmethionine decarboxylase proenzyme P0A7F6 SPED_ECOLI speD http://ecmdb.ca/proteins/P0A7F6.xml S-adenosyl-L-methionine + Hydrogen ion > Decarboxy-SAM + Carbon dioxide PW_R005960 Cadaverine + Decarboxy-SAM > Aminopropylcadaverine + 5'-Methylthioadenosine + Hydrogen ion PW_R005959 Decarboxy-SAM + Putrescine > 5'-Methylthioadenosine + Spermidine + Hydrogen ion PW_R005961