Abstract
Regulation of glutamine synthetase (GS) in the thermophilic green phototrophic bacterium, Chloroflexus aurantiacus, was studied. The enzyme was partially purified from cells grown photosynthetically in media with limiting (1 mM) or non-limiting (10 mM) NH+4-concentrations. GS preparations from both cell types were indistinguishable in respect to pH-optimum of GS-transferase activity, sensitivity to feedback modifiers (AMP, L-alanine, glycine) and lack of Mg-inhibition of transferase activity. In contrast to results obtained with a GS preparation from the facultatively phototrophic bacterium, Rhodopseudomonas sphaeroides, the catalytic properties of Chloroflexus GS did not change during incubation with snake venom phosphodiesterase suggesting the absence of in vivo regulation of Chloroflexus GS by adenylylation/deadenylylation.
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