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

Authors :
Paulin L
Vehmaanperä J
Nykänen I
Pösö H
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1983 Jul 29; Vol. 114 (2), pp. 779-84.
Publication Year :
1983

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.

Details

Language :
English
ISSN :
0006-291X
Volume :
114
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
6411092
Full Text :
https://doi.org/10.1016/0006-291x(83)90849-5