Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.2.2 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

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Rattus norvegicus
-

Storage Stability

Storage Stability Organism
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)

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

Subunits

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