Description_x000D_ General description_x000D_ L-Glutamine Synthetase from bacteria shows dodecameric structure comprising of 12 active sites. Each active site termed bifunnel, has an ATP and glutamate binding sites. The dodecamer is stabilized by two hexameric rings._x000D_ Application_x000D_ L-Glutamine Synthetase from Escherichia coli has been used in the synthesis of methylglutamine from methylammonium in E coli and in the glutamine synthetase protection activity of human thioredoxin peroxidase enzyme, AOE372._x000D_ L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli._x000D_ Biochem/physiol Actions_x000D_ L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine. It is a degradative enzyme for glutamic acid._x000D_ Nitrogen starvation dictates the expression of the glutamine synthetase (GS) gene in E. coli. GS plays a key role in ammonia assimilation in bacteria. Adenylylation of GS is catalyzed by adenylyltransferase. Adenylylation of GS modulates its catalytic functionality resulting in glutamine limitation in E coli._x000D_ Degradative enzyme for glutamic acid_x000D_ Unit Definition_x000D_ One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C._x000D_ Physical form_x000D_ Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts