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Literature summary for 6.3.2.3 extracted from

  • Tanaka, T.; Nishioka, T.; Oda, J.
    Nicked multifunctional loop of glutathione synthetase still protects the catalytic intermediate (1997), Arch. Biochem. Biophys., 339, 151-156.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information deletion mutant of the loop and mutant with a nicked multifunctional loop. Cleavage of the loop results in a drastic increase in activity, which is similar to the results for the loop deletion. High concentrations of ATP inhibit the wild-type enzyme, while both nicked and loopless enzyme are not inhibited Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP high concentrations inhibit the wild-type enzyme, while both nicked and loopless enzyme are not inhibited Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
ATP gamma-Glu-Cys, wild-type enzyme Escherichia coli
0.6
-
ATP mutant with a nicked loop Escherichia coli
0.7
-
gamma-Glu-Cys loopless mutant Escherichia coli
0.91
-
Gly wild-type enzyme Escherichia coli
1.54
-
ATP loopless mutant Escherichia coli
1.87
-
gamma-Glu-Cys mutant with a nicked loop Escherichia coli
23.3
-
Gly mutant with a nicked loop Escherichia coli
29.8
-
Gly loopless mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
JM109, wild-type, deletion mutant of the multifunctional loop and mutant with a nicked loop
-

Substrates and Products (Substrate)

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