Literature summary 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.

General Stability

EC Number	General Stability	Organism
6.3.2.3	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

EC Number	Organism	UniProt	Comment	Textmining
6.3.2.3	Escherichia coli	-	B	-
6.3.2.3	Escherichia coli B / ATCC 11303	-	B	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
6.3.2.3	-	Escherichia coli

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	-	?

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Release 2023.1 (January 2023)