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Literature summary extracted from

  • Seelig, G.F.; Simondsen, R.P.; Meister, A.
    Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits (1984), J. Biol. Chem., 259, 9345-9347.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.2 glutathione whole enzyme and large subunit inhibited Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.2.2 27700
-
 1 * 73000 + 1 * 27700, PAGE in presence of 50 mM DTT Rattus norvegicus
6.3.2.2 73000
-
 1 * 73000 + 1 * 27700, PAGE in presence of 50 mM DTT Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.2 kidney
-
 Rattus norvegicus
-

Storage Stability

EC Number Storage Stability Organism
6.3.2.2 4°C, 10 mM imidazole buffer, pH 8.4, 50 mM DTT, irreversible loss of activity after 4 h Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + L-Glu + L-Cys
-
 Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.2.2 dimer 1 * 73000 + 1 * 27700, PAGE in presence of 50 mM DTT Rattus norvegicus
6.3.2.2 More the heavy subunit contains all of the structural requirements for enzymatic activity and also for feedback inhibition by glutathione Rattus norvegicus