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Literature summary for 6.3.2.2 extracted from

  • Chang, L.; Chang, C.
    Biochemical regulation of the activity of gamma-glutamylcysteine synthetase from rat liver and kidney by glutathione (1994), Biochem. Mol. Biol. Int., 32, 697-703.
    View publication on PubMed
Search for more literature for 6.3.2.2

Inhibitors

Inhibitors Comment Organism Structure
cystamine
-
 Rattus norvegicus
glutathione
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4
-
 L-2-aminobutanoate L-Glu, kidney enzyme Rattus norvegicus
1.5
-
 L-2-aminobutanoate 2-aminobutanoate, kidney enzyme Rattus norvegicus
1.5
-
 L-2-aminobutanoate L-Glu, liver enzyme Rattus norvegicus
2.9
-
 2-aminobutyrate liver enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
-
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14.5
-
 liver enzyme Rattus norvegicus
19.2
-
 kidney enzyme Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-methyl-L-glutamate + 2-aminobutyrate
-
 Rattus norvegicus ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate
-
 ?
ATP + L-Glu + L-Cys
-
 Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?

Subunits

Subunits Comment Organism
? unlike kidney enzyme, most of liver enzyme is in a reduced form which does not have disulfide linkage between heavy and light chain Rattus norvegicus