|PROSITE documentation PDOC01033|
The nearly ubiquitous polyamines (putrescine, spermidine and spermine) are polycationic mediators of cell proliferation and differentiation whose functions likely provide both stability and neutralization for nucleic acids. The following polyamine biosynthetic enzymes are evolutionary related and contain a polyamine biosynthesis (PABS) domain :
The PABS domain consists of two subdomains: an N-terminal subdomain composed of six β-strands, and a Rossmann-like C-terminal subdomain (see <PDB:1INL>). The larger C-terminal catalytic core subdomain consists of a seven-stranded β-sheet flanked by nine α helices. This subdomain resembles a topology observed in a number of nucleotide and dinucleotide-binding enzymes, and in S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases (MTases) .
As a signature pattern, we selected a glycine-rich conserved region. We also developed a profile that spans both the N-terminal and the C-terminal catalytic subdomains.Last update:
October 2013 / Text and profile revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Hashimoto T. Tamaki K. Suzuki K. Yamada Y.|
|Title||Molecular cloning of plant spermidine synthases.|
|Source||Plant Cell Physiol. 39:73-79(1998).|
|2||Authors||Korolev S. Ikeguchi Y. Skarina T. Beasley S. Arrowsmith C. Edwards A. Joachimiak A. Pegg A.E. Savchenko A.|
|Title||The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.|
|Source||Nat. Struct. Biol. 9:27-31(2002).|