GTP-insensitive ornithine decarboxylase in acetobacteria able to synthesize spermine

Biochemical and Biophysical Research Communications
L PaulinH Pöso

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.

References

Jan 1, 1976·Annual Review of Biochemistry·C W Tabor, H Tabor
Aug 5, 1974·Biochemical and Biophysical Research Communications·E HölttäJ Pispa
Jun 9, 1972·Biochemical and Biophysical Research Communications·E HölttäJ Pispa
Jun 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·A Raina, S S Cohen

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