Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Protein Variants Comment Organism
6.3.2.3 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.3 0.24
-
 ATP gamma-Glu-Cys, wild-type enzyme Escherichia coli
6.3.2.3 0.6
-
 ATP mutant with a nicked loop Escherichia coli
6.3.2.3 0.7
-
 gamma-Glu-Cys loopless mutant Escherichia coli
6.3.2.3 0.91
-
 Gly wild-type enzyme Escherichia coli
6.3.2.3 1.54
-
 ATP loopless mutant Escherichia coli
6.3.2.3 1.87
-
 gamma-Glu-Cys mutant with a nicked loop Escherichia coli
6.3.2.3 23.3
-
 Gly mutant with a nicked loop Escherichia coli
6.3.2.3 29.8
-
 Gly loopless mutant Escherichia coli

Organism

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

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
-
 ?