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Literature summary for 6.3.1.2 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
Search for more literature for 6.3.1.2

Activating Compound

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

Metals/Ions

Metals/Ions Comment Organism Structure
Cl- increases the affinity of the enzyme 2fold to 4fold for Mg2+ or Mn2+ Bos taurus
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
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Bos taurus
-

Substrates and Products (Substrate)

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