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GTP-insensitive ornithine decarboxylase in acetobacteria able to synthesize spermine.

Authors
  • Paulin, L
  • Vehmaanperä, J
  • Nykänen, I
  • Pösö, H
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jul 29, 1983
Volume
114
Issue
2
Pages
779–784
Identifiers
PMID: 6411092
Source
Medline
License
Unknown

Abstract

Several Acetobacteria contained large amounts of spermine in addition to the putrescine and spermidine, which are the polyamines normally found in prokaryotes. A spermine synthase present in cell extracts of these Acetobacteria is the first example of this enzyme in prokaryotes. Dicyclohexylammonium sulphate inhibited both spermidine synthase and spermine synthase activities in Acetobacteria. Their ornithine decarboxylase was not stimulated by GTP nor inhibited by ppGpp and pppGpp (magic spots I and II) in contrast to ornithine decarboxylase of nearly all bacteria studied so far. However, their S-adenosyl-L-methionine decarboxylase resembled other prokaryotic adenosylmethionine decarboxylases in requiring Mg2+ ions in vitro for full activity.

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