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Literature summary for 6.3.2.3 extracted from

  • Hara, T.; Tanaka, T.; Kato, H.; Nishioka, T.; Oda, J.
    Site-directed mutagenesis of glutathione synthetase from Escherichia coli B: mapping of the gamma-glutamyl-L-cysteine-binding site (1995), Protein Eng., 8, 711-716.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information the mutant enzymes Arg86 and Asn283 are altered in their kinetic parameters, especially the Michaelis constant of gamma-Glu-Cys Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values of wild-type and mutant enzymes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and mutant enzymes
-
Escherichia coli
-
 B
-
Escherichia coli B / ATCC 11303
-
 B
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-Glu-L-Cys + Gly
-
 Escherichia coli ADP + phosphate + glutathione
-
 ?
ATP + gamma-Glu-L-Cys + Gly
-
 Escherichia coli B / ATCC 11303 ADP + phosphate + glutathione
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover-numbers of wild-type and mutant enzymes Escherichia coli