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

BRENDA support

Literature summary for 6.3.2.2 extracted from

  • Seelig, G.F.; Meister, A.
    gamma-Glutamylcysteine synthetase from erythrocytes (1984), Anal. Biochem., 141, 510-514.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
cystamine 7.5 mM MgCl2 + 7.5 mM L-Glu protect Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.35
-
ATP
-
Rattus norvegicus
1.2
-
L-Glu
-
Rattus norvegicus
1.5
-
L-2-aminobutanoate
-
Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
1 * 75000 + 1 * 25000, denaturing PAGE in presence of 50 mM DTT Rattus norvegicus
75000
-
1 * 75000 + 1 * 25000, denaturing PAGE in presence of 50 mM DTT Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
24.3
-
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + L-2-aminobutanoate
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
?
ATP + L-Glu + L-Cys
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
?

Subunits

Subunits Comment Organism
dimer 1 * 75000 + 1 * 25000, denaturing PAGE in presence of 50 mM DTT Rattus norvegicus