Literature summary for 6.3.2.3 extracted from

Kato, H.; Tanaka, T.; Nishioka, T.; Kimura, A.; Oda, J.
Role of cysteine residues in glutathione synthetase from Escherichia coli B (1988), J. Biol. Chem., 263, 11646-11651.

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Cloned(Commentary)

Cloned (Comment)	Organism
mutants Cys122Ala, Cys195Ala, Cys222Ala and Cys289Ala show no critical loss of activity. Multiple replacement of Cys residues, however, decreases enzymatic activity to 45-26% of the activity of the wild-type enzyme	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5,5'-dithiobis(2-nitrobenzoate)	Cys289 is the only amino acid residue reactive with DTNB. Modification of Cys289 with DTNB results in complete loss of the catalytic activity	Escherichia coli
NEM	-	Escherichia coli
PCMB	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild-type and mutant enzymes with Cys residues replaced by Ala	-

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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Release 2023.1 (January 2023)