S-Adenosylmethionine Decarboxylase from Escherichia Coli and from Saccharomyces Cerevisiae: Cloning and Overexpression of the Genes

  • K. Kashiwagi
  • S. K. Taneja
  • Q.-W. Xie
  • C. W. Tabor
  • H. Tabor
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 250)


S-Adenosylmethionine decarboxylase is a key enzyme in the biosynthesis of spermidine and spermine in both prokaryotes and eukaryotes.1 We first detected this enzyme in our initial studies on the biosynthesis of spermidine in E. coli2, 3; subsequently S-adenosylmethionine decarboxylase has been found widely distributed in bacteria, fungi, plants, and animal cells. The enzyme has been purified to homogeneity from E. coli,4, 5S. cerevisiae,6, 7 liver,8, 9 lymphocytes,11 and mammary gland.12


Reductive Amination Histidine Decarboxylase Methionine Adenosyltransferase Proenzyme Form Protein Cleavage Site 


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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • K. Kashiwagi
    • 1
  • S. K. Taneja
    • 1
  • Q.-W. Xie
    • 1
  • C. W. Tabor
    • 1
  • H. Tabor
    • 1
  1. 1.National Institute of Diabetes and Digestive and Kidney DiseasesNational Institutes of HealthBethesdaUSA

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