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Spermidine

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Spermidine
Names
IUPAC name
N-(3-aminopropyl)butane-1,4-diamine
Other names
1,5,10-triazadecane
Identifiers
3D model (JSmol)
ECHA InfoCard 100.004.264 Edit this at Wikidata
MeSH Spermidine
  • C(CCNCCCN)CN
Properties
C7H19N3
Molar mass 145.246
Density 0.925 g/mL at 25 °C
Melting point 22-25.0 °C
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Spermidine is a polyamine involved in cellular metabolism. It's known actions include: inhibition of neuronal nitric oxide synthase, nNOS[1], assisting the in vitro process of transcribing RNA, it stimulates T4 polynucleotide kinase and T7 RNA polymerase activity, it binds to and precipitates DNA and is utilized in purifying DNA binding proteins[2], as a polyamine plant growth regulator it is also a plant hormone promoting somatic embryogenesis[3] [4] [5] [6] [7] [8] [9]. Spermidine has also been found to reduce the amount of aging in yeast, flies, worms, and human immune cells by inducing autophagy[10]

Sources

  • Semen
  • Grapefruit

Biochemical actions

  • Inhibits neuronal nitric oxide synthase (nNOS)
  • Binds and precipitates DNA
  • May be used for purification of DNA-binding proteins
  • Stimulates T4 polynucleotide kinase and T7 RNA polymerase activity
  • Polyamine plant growth regulator

Some of the uses

  • Spermidine can be used in electroporation while transferring the DNA into the cell under the electrical impulse.
  • Stimulating autophagy.

See also

References

  1. ^ Hu J., Mahmoud M.I., el-Fakahany E.E., Polyamines inhibit nitric oxide synthase in rat cerebellum. Neurosci. Lett. 1994, 175, 41-5.
  2. ^ Wan C.Y., Wilkins T.A., Spermidine facilitates PCR amplification of target DNA. PCR Methods Appl. 1993, 3, 208-10.
  3. ^ Cull M., McHenry C.S., Preparation of extracts from prokaryotes. Methods Enzymol. 1990, 182, 147-53.
  4. ^ Blethen S.L., Boeker E.A., Snell E.E., Arginine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme. J. Biol. Chem. 1968, 243, 1671-7.
  5. ^ Wu W.H., Morris D.R., Biosynthetic arginine decarboxylase from Escherichia coli. Subunit interactions and the role of magnesium ion. J. Biol. Chem. 1973, 248, 1696-9.
  6. ^ Tabor C.W., Tabor H., Polyamines. Annu. Rev. Biochem. 1984, 53, 749-90.
  7. ^ Krug M.S., Berger S.L., First-strand cDNA synthesis primed with oligo(dT). Methods Enzymol. 1987, 152, 321-25.
  8. ^ Karkas J.D., Margulies L., Chargaff E., A DNA polymerase from embryos of Drosophila melanogaster. Purification and properties. J. Biol. Chem. 1975, 250, 8657-63.
  9. ^ Bouché J.P., The effects of spermidine on endonuclease inhibition by agarose contaminants. Anal. Biochem. 1981, 115, 42-5.
  10. ^ name=Nature Cell Biology>Tobias Eisenberg, Heide Knauer, Alexandra Schauer, Sabrina Büttner, Christoph Ruckenstuhl, Didac Carmona-Gutierrez, Julia Ring, Sabrina Schroeder, Christoph Magnes, Lucia Antonacci, Heike Fussi, Luiza Deszcz, Regina Hart, Elisabeth Schraml, Alfredo Criollo, Evgenia Megalou, Daniela Weiskopf, Peter Laun, Gino Heeren, Michael Breitenbach, Beatrix Grubeck-Loebenstein, Eva Herker, Birthe Fahrenkrog, Kai-Uwe Fröhlich, Frank Sinner, Nektarios Tavernarakis, Nadege Minois, Guido Kroemer, Frank Madeo (4 October 2009). "Induction of autophagy by spermidine promotes longevity,". Nature Cell Biology.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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