| The chemical and kinetic mechanism of low (LA) and high adenylylated (HA) E. coli and Anabaena 7120 glutamine synthetase (GS) was studied. Anabaena 7120 GS exhibited lower biosynthetic activity and higher transferase activity compared to LA E. coli GS. Their Michaelis constants were similar, except for ammonia.;In the presence of L-methionine-(S)-sulfoximine (MSOX), L-methionine sulfodiimine (MSOXD), and L-phosphinothricin the continuous wave (cw) EPR spectra of Mn (II) bound at the n;In the presence of chemically synthesized MSOXP the n;Pulsed EPR was used to study the n;Inhibition by AMP and CTP of Anabaena 7120 GS was studied kinetically. AMP inhibited by binding at the ATP active site and an AMP allosteric site. CTP did not inhibit. |
