Norspermidine

Last updated
Norspermidine
Bis(3-aminopropyl)amin Struktur.svg
Norspermidine molecule ball.png
Identifiers
3D model (JSmol)
3DMet
1071254
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.000.238
EC Number
  • 200-261-2
26839
KEGG
MeSH norspermidine
PubChem CID
RTECS number
  • JL9450000
UNII
UN number 2269
Properties
C6H17N3
Molar mass 131.223 g·mol−1
AppearanceColorless liquid
Odor Ichtyal, ammoniacal
Density 938 mg mL−1
Melting point −16 to 0 °C; 3 to 32 °F; 257 to 273 K
Boiling point 240.60 °C; 465.08 °F; 513.75 K
log P −0.826
1.481–1.482
Hazards
Safety data sheet fishersci.com
GHS pictograms GHS-pictogram-acid.svg GHS-pictogram-skull.svg
GHS Signal word Danger
H302, H311, H314, H317, H330
P260, P280, P284, P305+351+338, P310
Flash point 117 °C (243 °F; 390 K)
280 °C (536 °F; 553 K)
Lethal dose or concentration (LD, LC):
738 mg kg−1(oral, rat)
Related compounds
Related amines
Related compounds
 Agmatine
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Norspermidine is a polyamine of similar structure to the more common spermidine. While norspermidine has been found to occur naturally in some species of plants, [1] [2] bacteria, [3] and algae, [4] it is not known to exist in humans.

Norspermidine is being researched for use as a cancer medication. [5] [6]

Related Research Articles

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Spermidine chemical compound

Spermidine is a polyamine compound found in ribosomes and living tissues, and having various metabolic functions within organisms. It was originally isolated from semen.

Spermidine synthase class of enzymes

Spermidine synthase is an enzyme that catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The systematic name is S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase and it belongs to the group of aminopropyl transferases. It does not need any cofactors. Most spermidine synthases exist in solution as dimers.

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FEZ2 protein-coding gene in the species Homo sapiens

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PAOX protein-coding gene in the species Homo sapiens

Peroxisomal N(1)-acetyl-spermine/spermidine oxidase is an enzyme that in humans is encoded by the PAOX gene.

OAZ2 protein-coding gene in the species Homo sapiens

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Spermine oxidase (EC 1.5.3.16, PAOh1/SMO, AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming). This enzyme catalyses the following chemical reaction

References

  1. ↑ Rodriguez-Garay, B; et al. (1989). "Detection of Norspermidine and Norspermine in Medicago sativa L. (Alfalfa)". Plant Physiology. 89 (2): 525–529. doi:10.1104/pp.89.2.525. ISSN   0032-0889. PMC   1055875 . PMID   16666576.
  2. ↑ Hamana, K; et al. (1998). "Unusual polyamines in aquatic plants: the occurrence of homospermidine, norspermidine, thermospermine, norspermine, aminopropylhomospermidine, bis(aminopropyl)ethanediamine, and methylspermidine". Can. J. Bot. 76 (1): 130–133. doi:10.1139/cjb-76-1-130.
  3. ↑ Yamamoto, S; et al. (Apr 27, 1979). "Occurrence of norspermidine in some species of genera Vibrio and Beneckea". Biochem Biophys Res Commun. 87 (4): 1102–1108. doi:10.1016/S0006-291X(79)80021-2. PMID   313792.
  4. ↑ Hamana, K; Matsuzaki, S (1982). "Widespread Occurrence of Norspermidine and Norspermine in Eukaryotic Algae". J. Biochem. 91 (4): 1321–1328. ISSN   0021-924X. PMID   7096289.
  5. ↑ Prakash, NJ; et al. (1988). "Antitumor activity of norspermidine, a structural homologue of the natural polyamine spermidine". Anticancer Res. 8 (4): 563–568. PMID   3140710.
  6. ↑ Sunkara, PS; et al. (1988). "Mechanism of antitumor activity of norspermidine, a structural homologue of spermidine". Adv Exp Med Biol. 250: 707–716. doi:10.1007/978-1-4684-5637-0_62. PMID   3255245.
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