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Literature summary for 6.3.2.2 extracted from

  • Chang, L.
    The functional involvement of Lys-38 in the heavy subunit of rat kidney gamma-glutamylcysteine synthetase: chemical modification and mutagenesis studies (1996), J. Protein Chem., 15, 321-326.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K38A mutant enzyme Lys38Arg: small changes in the catalytic properties, mutant enzyme K38N and K38E show marked decrease in enzymatic activity and about 2fold increase in Km for Glu Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
Trinitrobenzene sulfonate addition of 10 mM Mg2+ results in a 16fold increase of inactivation rate, Lys-38 in the heavy subunit is significantly modified in presence of Mg2+ Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
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Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + L-Cys
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Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
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