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

BRENDA support

Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.3 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

EC Number Inhibitors Comment Organism Structure
6.3.2.3 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
6.3.2.3 NEM
-
Escherichia coli
6.3.2.3 PCMB
-
Escherichia coli

Organism

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

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
-
?