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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.3 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

EC Number Inhibitors Comment Organism Structure
6.3.2.3 5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli

KM Value [mM]

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

Organism

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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