Subsystem: Polyamine Metabolism

This subsystem's description is:

Polyamines are essential and ancient small polycation metabolites required for cell growth and proliferation and are found in most if not all bacterial, fungal, animal and plant cells (Illingworth et al., 2003; Yoshida et al., 2004; Tabor & Tabor, 1985). The most common polyamines are putrescine (1,4-diaminobutane) and spermidine; spermine is present largely in eukaryotes. In some microbial species (Vibrio, a number of archaea and thermophilic bacteria) the major polyamine is norspermidine. The genes for norspermidine synthesis are present in the genomes of many members of the proteobacteria and of a few members of the deinococci, bacteroidetes, cyanobacteria, and gram-positive bacteria (Karatan et al., 2005)

Putrescine is synthesized from ornithine by ornithine decarboxylase (OrnDC) or from arginine by the sequential actions of (i) arginine decarboxylase and agmatinase (ArgDC+AUH) or (ii) arginine decarboxylase, Agmatine deiminase and N-carbamoylputrescine amidase (ArgDC+AIH+CPA).
In well studied organisms, such as E. coli, two types of ornithine decarboxylase and arginine decarboxylase can be distinguished: biodegradative (induced) and biosynthetic (constitutive) (Tabor and Tabor, 1985). Extrapolation of these data has not been attempted for the majority of organisms in this SS.

Spermidine synthase (SPDS) synthesizes spermidine from putrescine by the addition of an aminopropyl group acquired from decarboxylated S-adenosylmethionine formed by S-adenosyl-methionine decarboxylase (Woolridge, 1999). Similarly, spermine is formed from spermidine by spermine synthase or spermidine synthase through addition of another aminopropyl group. Spermidine and spermine can be further metabolized by acetylation (Casero et al., 1993). In addition, uptake systems for putrescine, spermidine and spermine has been described for various microorganisms. In contrast to putrescine and spermidine, spermine is normally not present in media or under natural conditions.

Several widely distributed Polyamine transport systems have been characterized (Igarashi et al., 1999; Woolridge et al., 1997). In the absence of polyamine biosynthetic pathways one or more polyamine transport systems is likely to be present – but in many cases potential gene candidates were not annotated as such: impossible to predict a transporter’s substrate based on sequence alone.

Polyamine metabolism has been targeted for therapeutic or preventative intervention in the treatment of certain diseases, based on the observation of increased polyamine concentration in a variety of diseases and parasitic infections (reviewed in Wallace, et al., 2004).

See also related subsystems: Arginine Putrescine and 4-aminobutyrate degradation; Putrescine utilization cluster; Biofilm formation in Vibrio.

This Subsystem has been originally encoded by Ines Thiele (UCSD), whose excellent contribution we gratefully acknowledge.


Casero, R. A., Jr., and A. E. Pegg. 1993. Spermidine/spermine N1-acetyltransferase--the turning point in polyamine metabolism. Faseb J 7:653-61.

Igarashi K and Kashiwagi K. Polyamine Modulon in Escherichia coli: Genes Involved in the Stimulation of Cell Growth by Polyamines. J Biochem (Tokyo). 2006 Jan;139(1):11-6.

Igarashi, K., and K. Kashiwagi. 1999. Polyamine transport in bacteria and yeast. Biochem J 344 Pt 3:633-42.

Igarashi K., K. Itob , K.Kashiwagia. Polyamine uptake systems in Escherichia coli. Res. Microbiol. 152 (2001) 271–278

Illingworth, C., M.J. Mayer, K. Elliott, C. Hanfrey, N.J. Walton, A.J. Michael. The diverse bacterial origins of the Arabidopsis polyamine biosynthetic pathway. FEBS Letters 549 (2003) 26-30

Ishii, I., H. Takada, K. Terao, T. Kakegawa, K. Igarashi, and S. Hirose. 1994. Decrease in spermidine content during logarithmic phase of cell growth delays spore formation of Bacillus subtilis. Cell Mol Biol (Noisy-le-grand) 40:925-31.

Karatan E, Duncan TR, Watnick PI. 2005. NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine. J Bacteriol, 187(21):7434-43.

Tabor, C. W., and H. Tabor. 1985. Polyamines in microorganisms. Microbiol Rev 49:81-99.
Tomitori, H., K. Kashiwagi, K. Sakata, Y. Kakinuma, and K. Igarashi. 1999. Identification of a gene for a polyamine transport protein in yeast. J Biol Chem 274:3265-7.

Wallace, H. M., and A. V. Fraser. 2004. Inhibitors of polyamine metabolism: review article. Amino Acids 26:353-65.

Woolridge, D. P., J. D. Martinez, D. E. Stringer, and E. W. Gerner. 1999. Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis. Biochem J 340 (Pt 3):753-8.

Woolridge, D. P., N. Vazquez-Laslop, P. N. Markham, M. S. Chevalier, E. W. Gerner, and A. A. Neyfakh. 1997. Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt. J Biol Chem 272:8864-6.

Yoshida M, Kashiwagi K, Shigemasa A, Taniguchi S, Yamamoto K, Makinoshima H, Ishihama A, Igarashi K. 2004. A unifying model for the role of polyamines in bacterial cell growth, the polyamine modulon. J Biol Chem, 279(44):46008-13.

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