page_title: Glutamine synthetase
hierarchical_section_title: Glutamine synthetase
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 2gls code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 2gls code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 2gls registreert is.
context_page_description: Glutamine synthetase is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:
  Glutamate + ATP + NH₃ → Glutamine + ADP + phosphate
  Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites.
  Other reactions may take place via GS. Competition between ammonium ion and water, their binding affinities, and the concentration of ammonium ion, influences glutamine synthesis and glutamine hydrolysis. Glutamine is formed if an ammonium ion attacks the acyl-phosphate intermediate, while glutamate is remade if water attacks the intermediate. Ammonium ion binds more strongly than water to GS due to electrostatic forces between a cation and a negatively charged pocket. Another possible reaction is upon NH₂OH binding to GS, rather than NH₄+, yields γ-glutamylhydroxamate.
context_section_description: Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:
  Glutamate + ATP + NH₃ → Glutamine + ADP + phosphate 
  Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites.
  Other reactions may take place via GS. Competition between ammonium ion and water, their binding affinities, and the concentration of ammonium ion, influences glutamine synthesis and glutamine hydrolysis. Glutamine is formed if an ammonium ion attacks the acyl-phosphate intermediate, while glutamate is remade if water attacks the intermediate.  Ammonium ion binds more strongly than water to GS due to electrostatic forces between a cation and a negatively charged pocket. Another possible reaction is upon NH₂OH binding to GS, rather than NH₄+, yields γ-glutamylhydroxamate.
caption: 12-subunit enzyme glutamine synthetase from Salmonella typhimurium.[2]
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