Enzyme
6.3.2.2 - Glutamate--cysteine ligase
Alternative Name(s)
- Gamma-glutamylcysteine synthetase.
- Gamma-glutamyl-L-cysteine synthetase.
Catalytic Activity
ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-glutamyl-L-cysteine + phosphate
Cofactors
There are no Cofactors for this Enzyme
Reaction Mechanism
There are no Reaction Mechanism for this Enzyme
Reaction Parameters
-
Kinetic Parameters
Organism KM Value [mM] Substrate Comment Synechocystis sp. 0.0086 ATP pH 7.5, 25°C, mutant R248K Pseudoalteromonas haloplanktis 0.044 ATP pH 8.0, 15°C, recombinant enzyme Escherichia coli 46.6 ATP pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y -
Temperature
There are no reaction parameters information for this Enzyme.
-
pH
Organism pH Range Comment Nicotiana tabacum 7 - 9 50% of maximal activity at pH 7.0 and pH 9.0 Pseudoalteromonas haloplanktis 7 - 9 narrow pH range, highest activity at pH 7.8-8.6
Associated Proteins
Citations
- Covalent Targeting of Glutamate Cysteine Ligase to Inhibit Glutathione Synthesis
- Characterization of a glutamate-cysteine ligase in Bombyx mori.
- Involvement of Glutamate Cysteine Ligase Genes in Tolerance to Emamectin Benzoate in Spodoptera frugiperda and Their Putative Regulatory Mechanisms.
- Characterization of a glutamate-cysteine ligase in Bombyx mori
- Endogenous benzoic acid interferes with the signatures of amino acids and thiol compounds through perturbing N-methyltransferase, glutamate-cysteine ligase, and glutathione S-transferase activity in dairy products
- Characterization of glutamate-cysteine ligase and glutathione synthetase from the δ-proteobacterium Myxococcus xanthus.
- Glutamate-cysteine ligase catalytic and its modifier function as novel immunotargets in gastric adenocarcinoma.
- Uric acid effects on glutathione metabolism estimated by induction of glutamate-cysteine ligase, glutathione reductase and glutathione synthetase in mouse J744A.1 macrophage cell line.
- Genetic variation at the catalytic subunit of glutamate cysteine ligase contributes to the susceptibility to sporadic colorectal cancer: a pilot study.
- Genetic Variation at the Catalytic Subunit of Glutamate Cysteine Ligase Contributes to the Susceptibility to Colorectal Cancer: A Pilot Study
- Endogenous benzoic acid interferes with the signatures of amino acids and thiol compounds through perturbing N-methyltransferase, glutamate-cysteine ligase, and glutathione S-transferase activity in dairy products.