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Literature summary for 6.3.2.3 extracted from

  • Tanaka, T.; Kato, H.; Nishioka, T.; Oda, J.
    Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction (1992), Biochemistry, 31, 2259-2265.
    View publication on PubMed

General Stability

General Stability Organism
proteolysis by arginyl endopeptidase or trypsin causes a time-dependent decrease in activity. Only one peptide bond between Arg233 and Gly234 in the loop is cleaved Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
B
-
Escherichia coli B / ATCC 11303
-
B
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

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
-
?