Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum

FEBS Lett. 2009 Nov 3;583(21):3519-24. doi: 10.1016/j.febslet.2009.10.014. Epub 2009 Oct 12.


Polyamines are ubiquitously present in all organisms. In addition to the common polyamines, thermophilic archaea synthesize long-chain polyamines. In the present study polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum were cloned and their substrate specificity was analyzed. The polyamine synthase HbSpeE II from H. butylicus synthesized long-chain polyamines with high activity using the same mechanism that is used by a wide range of organisms to synthesize common polyamines, in which the aminopropyl residue derives from decarboxylated S-adenosylmethionine. This is the first polyamine synthase described that synthesizes a polyamine longer than a tetramine with high activity.

MeSH terms

  • Cloning, Molecular
  • Ligases / biosynthesis
  • Ligases / genetics
  • Ligases / metabolism*
  • Phylogeny
  • Polyamines / analysis
  • Polyamines / chemistry*
  • Polyamines / metabolism*
  • Pyrobaculum / enzymology*
  • Pyrodictiaceae / enzymology*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Analysis, DNA
  • Substrate Specificity


  • Polyamines
  • Recombinant Proteins
  • Ligases