N1-Acetylspermine is a monoacetylated derivative of spermine , an endogenous polyamine synthesized from spermidine , that displays lower Km and higher Vmax values than spermine, making it a better substrate of polyamine oxidase than the non-acetylated polyamine. [1] Spermine is required for eukaryotic cell growth and protein synthesis and is involved in the modulation of calcium-dependent immune processes. [2][3] N1-Acetylspermine has been used to study the uptake of the anticancer polyamine analog bleomycin-A5 by the human carnitine transporter SLC22A16.[4]
Reference:
[1]. Bolkenius, F.N., and Seiler, N. Acetylderivatives as intermediates in polyamine catabolism. International Journal of Biochemistry 13(3), 287-292 (1981).
[2]. Wallace, H.M., Fraser, A.V., and Hughes, A. A perspective of polyamine metabolism. Biochemistry Journal 376(Pt 1), 1-14 (2003).
[3]. Igarashi, K., and Kashiwagi, K. Polyamines: Mysterious modulators of cellular functions. Biochemical and Biophysical Research Communications 271(3), 559-564 (2000).
[4]. Aouida, M., Poulin, R., and Ramotar, D. The human carnitine transporter SLC22A16 mediates high affinity uptake of the anticancer polyamine analogue bleomycin-A5. The Journal of Biological Chemisty 285(9), 6275-6284 (2010).