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Home > Art, Film & Photography > EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase
EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase

EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase


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Chapters: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase, Aspartate-Ammonia Ligase, Glutamate-Ethylamine Ligase, Glutamate-Putrescine Ligase, 4-Methyleneglutamate-Ammonia Ligase, Trypanothione Synthase, Amide Synthases. Source: Wikipedia. Pages: 34. Not illustrated. Free updates online. Purchase includes a free trial membership in the publisher's book club where you can select from more than a million books without charge. Excerpt: 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 + H2O 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 -glutamylhdyroxamate. Glutamine Synthetase 12 subunitsGlutamine Synthetase can be composed of 8, 10, or 12 identical subunits separated into two face-to-face rings.. Bacterial GS are dodecamers with 12 active sites between each monomer. Each active site creates a bifunnel which is the site of three distinct substrate binding sites: nucleotide, ammonium ion, and amino acid. ATP binds to the top of the bifunnel that opens to the external surface of GS. Glutamate binds...More: http: //booksllc.net/?id=259967


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Product Details
  • ISBN-13: 9781157093497
  • Publisher: Books LLC
  • Publisher Imprint: Books LLC
  • Height: 152 mm
  • Sub Title: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase
  • Width: 229 mm
  • ISBN-10: 1157093493
  • Publisher Date: 15 Sep 2010
  • Binding: Paperback
  • Spine Width: 2 mm
  • Weight: 68 gr


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EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase
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EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase
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EC 6.3.1 EC 6.3.1: Glutamine Synthetase, D-Aspartate Ligase, Glutathionylspermiglutamine Synthetase, D-Aspartate Ligase, Glutathionylspermidine Synthase, Nad+ Synthase

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