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Literature summary for 6.3.2.3 extracted from

  • Gupta, S.; Srivastava, A.K.; Banu, N.
    Setaria cervi: kinetic studies of filarial glutathione synthetase by high performance liquid chromatography (2005), Exp. Parasitol., 111, 137-141.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-cystine 1 mM, 11% inhibition Setaria cervi
NEM IC50: 9 mM, almost complete inhibition at 20 mM Setaria cervi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the KM-value for gamma-L-Glu-L-Cys gives a distinctly nonlinear double-reciprocal plot Setaria cervi
0.41
-
Gly 37°C Setaria cervi
0.95
-
ATP 37°C Setaria cervi

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Setaria cervi 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + gamma-L-Glu-L-Cys + Gly Setaria cervi enzyme catalyzes the final step of glutathione biosynthesis ADP + phosphate + glutathione
-
?

Organism

Organism UniProt Comment Textmining
Setaria cervi
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-L-Glu-L-Cys + Gly
-
Setaria cervi ADP + phosphate + glutathione
-
?
ATP + gamma-L-Glu-L-Cys + Gly enzyme catalyzes the final step of glutathione biosynthesis Setaria cervi ADP + phosphate + glutathione
-
?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
9
-
IC50: 9 mM, almost complete inhibition at 20 mM Setaria cervi NEM