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Literature summary extracted from

  • Maurizi, M.R.; Pinkofsky, H.B.; Ginsburg, A.
    ADP, chloride ion, and metal ion binding to bovine brain glutamine synthetase (1987), Biochemistry, 26, 5023-5031.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.1.2 arsenate activates gamma-glutamyl transferase reaction Bos taurus
6.3.1.2 L-glutamate causes conformational changes similar to those produced by Cl-binding Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.2 Cl- increases the affinity of the enzyme 2fold to 4fold for Mg2+ or Mn2+ Bos taurus
6.3.1.2 Mg2+ the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression Bos taurus
6.3.1.2 Mn2+ the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.2 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.2
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.1.2 brain
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.2 ATP + L-Glu + NH4+
-
 Bos taurus ADP + phosphate + L-Gln
-
 ?