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Enzyme Nomenclature
Information on EC 6.3.2.2 - glutamate-cysteine ligase
for references in articles please use BRENDA:EC6.3.2.2
Word Map on EC 6.3.2.2
- 6.3.2.2
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ganglion
- retina
- injury
- peroxidase
- sulfoximine
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buthionine
- heme
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plexiform
- superoxide
- thiols
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oxygenase-1
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amacrine
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tomography
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neuroprotective
- gssg
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coherence
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nadph:quinone
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2-related
- transpeptidase
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photoreceptors
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erythroid
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cytoprotective
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dentate
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macular
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neurogenesis
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intravitreal
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nrf2-dependent
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l-buthionine-s,r-sulfoximine
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nrf2-mediated
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nf-e2-related
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peripapillary
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kelch-like
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fovea
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gsh-dependent
- tert-butylhydroquinone
- gamma-glutamyltranspeptidase
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somata
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nrf2-are
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glutathione-related
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ech-associated
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oxidoreductase-1
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spectral-domain
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sd-oct
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nrf2-regulated
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subgranular
- phytochelatins
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factor-erythroid
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b-waves
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gsh-related
- biotechnology
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gsh-depleting
- synthesis
- medicine
- drug development
- pharmacology
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
6.3.2.2
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RECOMMENDED NAME
GeneOntology No.
glutamate-cysteine ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
tri tri sequential mechanism
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
bi bi uni uni ping pong mechanism, with glutamyl-enzyme as intermediate before the addition of cys and the release of gamma-glutamylcysteine
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
partially random mechanism in which ATP is the obligatory first substrate and both amino acids bind in a random order to the enzyme*ATP complex. Formation of the enzyme*substrate quarternary complex is necessary prior to release of products
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, catalytic mechanism and substrate binding
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
no conserved cysteine residue in the active site
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
no conserved cysteine residue in the active site
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
P97494;, Q97SC0;
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, catalytic mechanism, active site and substrate binding, Lys38 is an active site residue in the glutamyl binding site, His150 is essential for activity
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Cys553 is not the active site residue
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
rapid equilibrium random ter-reactant mechanism, substrate binding modeling, active site model
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
substrate binding mechanism and catalytic site structure determination and analysis, Arg127 and conserved Cys249 are involved
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
rapid equilibrium random ter-reactant mechanism, substrate binding modeling, Cys319 is an active site cysteine not essential for activity; reaction and kinetic mechanism, modeling
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
reaction mechanism via phosphorylated glutamate intermediate
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
reaction mechanism
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
reaction mechanism, overview
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
reaction mechanism
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
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carboxylic acid amide formation
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Ligation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:L-cysteine gamma-ligase (ADP-forming)
Can use L-aminohexanoate in place of glutamate.
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CAS REGISTRY NUMBER
COMMENTARY
9023-64-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes GCLC and GCLM encoding catalytic heavy chain subunit and modifier light chain subunits
C1KBE8, C1KBE7
UniProt
genes I79_010621 and I79_022778 encoding catalytic and regulatory subunits
G3HIY9, G3IG96
UniProt
Escherichia coli B / ATCC 11303
symbiotic sea anemone, genes gclC and gclM encoding the catalytic and the modifier subunits of the enzyme
UniProt
enriched by recombinant DNA techniques in its content of gamma-glutamylcysteine synthetase, strain W, strain KM
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1143, 649413, 649655, 649660, 650713, 651391, 651996, 653714, 653993, 661855, 671216, 671223, 672904, 674140, 675918, 676099, 692442, 692444, 694609, 703592, 703799, 704577, 704665, 704751, 705264, 705828, 706834, 714265, 715088, 716235, 726668
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activity of the gamma-glutamylcysteine synthetase promoter decreases after indomethacin treatment; leukemia cell. Cells show increased expression of gamma-glutamylcysteine synthetase. Expression decreases by indomethacin treatment
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enzyme consists of a catalytic GCLC and a modulatory GCLM subunit encoded by 2 separate gcl genes
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genes GCLC and GCLM encoding catalytic and modifier subunits
UniProt
genes GCLC and GCLM encoding heavy and light chain subunits
UniProt
healthy individuals and chronic obstructive pulmonary disease patients, genes gclC and gclM encoding the two subunits of the enzyme
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Japanese individuals and patients with methamphetamine dependence and induced psychosis, genes gclC and gclM encoding the catalytic and the modifier subunit of the enzyme
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1145, 652979, 660892, 661811, 662412, 663372, 671927, 674653, 676160, 703091, 703807, 704707, 706087, 706829, 715088, 726668, 727274
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genes GCLC and GCLM encoding catalytic heavy chain subunit and modifier light chain subunits
P97494, O09172
UniProt
wild-type and overexpressing gamma-glutamylcysteine synthetase
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1118, 1119, 1121, 1122, 1123, 1124, 1125, 1129, 1130, 1132, 1133, 1134, 1135, 1136, 1138, 1139, 1144, 1147, 1150, 649315, 652304, 661014, 663435, 673803, 703167, 704924, 706835, 706846, 715084, 726668
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genes GCLC and GCLM encoding heavy and light chain subunits
UniProt
bifunctional glutamate-cysteine ligase and glutathione synthetase
UniProt
bifunctional glutamate-cysteine ligase and glutathione synthetase
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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in eukaryotes gamma -glutamylcysteine synthetase and glutathione synthetase, EC 6.3.2.3, activities are encoded by two distinct enzymes In some prokaryotes, such as Escherichia coli and Vibrio cholerae, separate enzymes exist for these two reactions. However, in some prokaryotes, such as Streptococcus agalactiae, Pasteurella multicoda and Listeria monocytogenes, both of these activities are encoded by a single bifunctional enzyme, GshF. Evolution of gamma-GCS has occurred by convergent evolution in three different lineages with no significant sequence similarities between the lineages, the Escherichia coli enzyme belongs to lineage I
evolution
Synechocystis GCL is part of the plant-like GCL family, the Synechocystis enzyme lacks the redox regulation associated with the plant enzymes and functions as a monomeric protein, indicating that evolution of redox regulation occurs later in the green lineage
evolution
Gsh1 belongs to the eu-GC superfamily; the enzyme encoded by GSH1 belongs to the eu-GC superfamily
malfunction
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using GCLC knockout murine embryonic fibroblasts, addition of cysteine to catalytic subunit GCLC null cells results in a marked decrease in regulatory subunit GCLM mRNA levels despite the absence of GSH
malfunction
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erythrocytes from gclm-/- mice show greatly reduced intracellular glutathione. Prolonged incubation results in complete lysis of gclm-/- erythrocytes, which can be reversed by exogenous delivery of the antioxidant Trolox. Phenylhydrazine-induced oxidative stress in glcm-/- causes dramatically increased hemolysis, markedly larger accumulations of injured erythrocytes in the spleen, erythrocyte-derived pigment hemosiderin in kidney tubules, and diminished kidney function compared to wild-type mice, phenotype, overview. Regulatory subunit GCLM-deficient erythrocytes are more prone to Ca2+-dependent suicidal cell death ex vivo. Without additional oxidative stress, the mutant animals are able to survive by slightly ramping up their generation of new erythrocytes
malfunction
GSH can be depleted through the specific downregulation of the GCL levels by hammerhead ribozyme
malfunction
G3HIY9; G3IG96;
overexpression of subunit Gclc-X2 leads to upregulation of the proteins Abcf1, Fkbp4, and Eif3h, as well as to downregulation of protein Lamb1. There is no significant difference in growth rate during exponential phase at 32C between Gclm+ or Gclc-X2+ populations and the wild-type population. A higher cell proliferation observed in the Gclc overexpressing population. Gclc-X2 but not Gclm overexpression increases Gcl activity
malfunction
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in patients with systemic lupus erythematosus (SLE), the levels of enzyme GCL activity and reduced glutathione (GSH) decrease, while thioredoxin (TRX) and oxidized glutathione (GSSG) levels increase when compared with those in the healthy controls. GSH concentrations and GCL activity levels negatively correlate with the SLE disease activity index and erythrocyte sedimentation rate. Patients with SLE and nephritis have lower levels of GSH and GCL activity and higher levels of TRX and GSSG compared with those in SLE patients without nephritis. Insufficient levels of GSH and GCL activity in PBMCs may contribute to the pathogenesis of SLE. A negative association of GSH levels with T-lymphocyte and CD4+ and CD8+ lymphocyte subset apoptosis, and intracellular activated caspase?3 may supports the role of GSH in the alteration of apoptosis of T lymphocytes in the SLE disease state. GSH is involved in the depletion of CD4+ T lymphocytes in patients with SLE
malfunction
a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH
malfunction
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a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH
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metabolism
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the regulation of GCL, especially the catalytic subunit, with stress may be compromised in aging muscles. In aging muscles with 14 days of hind-limb unloading, failure to maintain the accelerated GCL catalytic subunit production and GCL activity, are associated with the GSH depletion
metabolism
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biosynthesis of GSH occurs by two sequential ATP-dependent enzymatic steps. The first enzyme, gamma -glutamylcysteine synthetase ligates glutamate and cysteine to yield gamma -glutamylcysteine. Glutathione synthetase, EC 6.3.2.3, the second enzyme, then catalyses the addition of glycine to yield glutathione
metabolism
the enzyme catalyses the first step of glutathione biosynthesis by forming gamma-glutamyl-cysteine from glutamate and cysteine in an ATP-dependent reaction. Formation of gamma-glutamyl-cysteine is not the rate-limiting step of glutathione biosynthesis in Pseudoalteromonas haloplanktis
metabolism
G3HIY9; G3IG96;
the enzyme catalyzes the first step in the glutathione biosynthesis
metabolism
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glutamate cysteine ligase (GCL) catalyzes the first and rate-limiting step of glutathione, GSH, biosynthesis. The associations between GSH levels and GCL activity with demographic characteristics, clinical manifestations and laboratory parameters in peripheral blood mononuclear cells (PBMCs) are analyzed, overview
metabolism
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the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
metabolism
C1KBE8; C1KBE7;
glutamate-cysteine ligase is one of the two enzymes involved in the synthesis of glutathione (GSH). This tripeptide is synthesized by two consecutive enzymatic reactions. Ligation of glutamate and cysteine,the rate-limiting step of GSH de novo synthesis, is catalyzed by glutamate-cysteine ligase. The following addition of glycine to the dipeptide is catalyzed by glutathione synthetase, EC 6.3.2.3
metabolism
P97494; O09172;
certain carotenoids induce the Gcl mRNA expression in RAW264 cells and subsequently the GCL protein expression, which concomitantly enhances the intracellular GSH level, in a JNK pathway-related manner
metabolism
the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine; the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine. GSH production occurs through two mechanisms: de novo synthesis and GSSG recycling. De novo synthesis occurs in a two-step reaction catalyzed by the two separate enzymes, glutamate cysteine ligase and glutathione synthetase, EC 6.3.2.3
metabolism
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the enzyme catalyses the first step of glutathione biosynthesis by forming gamma-glutamyl-cysteine from glutamate and cysteine in an ATP-dependent reaction. Formation of gamma-glutamyl-cysteine is not the rate-limiting step of glutathione biosynthesis in Pseudoalteromonas haloplanktis
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metabolism
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the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine; the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine. GSH production occurs through two mechanisms: de novo synthesis and GSSG recycling. De novo synthesis occurs in a two-step reaction catalyzed by the two separate enzymes, glutamate cysteine ligase and glutathione synthetase, EC 6.3.2.3
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metabolism
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the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
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physiological function
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mice lacking the glutamate-cysteine ligase modifier subunit show an increase in myocardial ischaemia-reperfusion injury and apoptosis in ischaemic myocardium. A decrease in mitochondrial glutathione levels in ischaemic myocardium is more pronounced in mice lacking the glutamate-cysteine ligase modifier subunit than in control. The ESR signal intensity of the dimethyl-1-pyrroline-N-oxide-hydroxyl radical adducts in ischaemic myocardium is higher in mice lacking the glutamate-cysteine ligase modifier subunit than in control. Hypoxia-reoxygenation induces greater mitochondrial damage in cultured cardiomyocytes from mice lacking the glutamate-cysteine ligase modifier subunit
physiological function
in a strain lacking GshA activity, diamide, a thiol-specific oxidant, significantly inhibits the growth of cells in comparison to those of the wild type. In contrast, 1.0 mM paraquat, 0.1 mM t-butyl hydroperoxide, 0.5 mM hydrogen peroxide, and 0.01 mM menadione have a much less pronounced effect on growth
physiological function
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model to explain adenosine triphosphate depletion during cystinosis. In the absence of cysteine, enzyme gamma-glutamyl cysteine synthetase forms 5-oxoproline, and the 5-oxoproline is converted into glutamate by the ATP-dependant enzyme, 5-oxoprolinase. Thus, in cysteine-limiting conditions, glutamate is cycled back into glutamate via 5-oxoproline at the cost of two ATP molecules without production of glutathione and this is the cause of the decreased levels of glutathione synthesis, as well as the ATP depletion observed in these cells. The model is also compatible with the differences seen in the human patients and the mouse model of cystinosis, where renal failure is not observed
physiological function
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the high resistance of MYCN-amplified neuroblastoma cells against oxidative damage can be accounted for by their greater expression of both the mRNA and protein of the catalytic subunit of glutamate-cysteine ligase, the rate-limiting step in GSH biosynthesis. MYCN directly binds to an E-box containing GCL catalytic subunit promoter and over-expression of MYCN in MYCN-non-amplified cells stimulates GCL catalytic subunit expression and provides resistance to oxidative damage. Knock-down of MYCN in MYCN-amplified cells decreases GCL catalytic subunit expression and sensitizes them to oxidative damage. GCL catalytic subunit knock-down enhances the vulnerability of MYCN-amplified cells to oxidative damage
physiological function
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generation of GSH1 null mutants in Leishmania infantum. Removal of even a single wild-type allelic copy of GSH1 invariably leads to the generation of an extra copy of GSH1, maintaining two intact wild-type alleles. By first supplementing the parasites with a rescue plasmid, both a single and null chromosomal GSH1 mutant can be obtained. Parasites with one intact GSH1 chromosomal allele lose the rescuing plasmid but not the double knockout, when grown in the absence of antibiotic, indicating the essentiality of the GSH1 gene. Heterozygous mutants with one allele inactivated transcribe less GSH1 mRNA and synthesize less glutathione and trypanothione. These mutants are more susceptible to oxidative stresses in vitro as promastigotes and show decreased survival inside activated macrophages producing reactive oxygen or nitrogen species. These mutants show a significant decreased survival in the presence of antimony
physiological function
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transfection of COV-434 granulosa tumour cell with vectors designed for the constitutive expression of Gcl catalytic subunit, Gcl modifier subunit, or both Gcl catalytic subunit and Gcl modifier subunit. GCL protein and enzymatic activity and total GSH levels are significantly increased in the GCL subunit-transfected cells. GCL-transfected cells are resistant to cell killing by treatment with hydrogen peroxide compared to control cells. In all the GCL subunit-transfected cell lines cell viability declines less than in control 1-8 h after 0.5 mM hydrogen peroxide treatment. In cells irradiated with 0, 1 or 5 Gy of g-rays, there is a dose-dependent increase in reactive oxygen species within 30 min in all cell lines, this effect is significantly attenuated in Gcl-transfected cells. Apoptosis is significantly decreased in irradiated Gclc-transfected cells compared to irradiated control cells
physiological function
knockdown of gamma-glutamylcysteine synthetase heavy chain subunit by an adenovirus vector with short hairpin RNA against GCSh. Three days infection of GCSh-shRNA and CYP3A4 simultaneously with H4IIE cells decreases the intracellular GSH level by 50-60% without affecting the expression level of CYP3A4. Using this cell-based system sensitive to the cytotoxicity of reactive metabolites, drugs known for their hepatotoxicity are evaluated. Troglitazone, flutamide, and acetaminophen cause significant decreases of cell viability in CYP3A4/GCSh-shRNA group compared to the other groups such as GFP, CYP3A4, GFP/GCSh-shRNA, indicating that reactive metabolites produced by CYP3A4 and subsequently conjugated by GSH are involved in the cytotoxicity
physiological function
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fibroblast growth factor 9 upregulates gamma-GCS and HO-1 expression to protect cortical and dopaminergic neurons from 1-methyl-4-phenylpyridinium-induced oxidative insult. Inhibition of gamma-GCS or HO-1 prevents the inhibitory effect of fibroblast growth factor 9 on 1-methyl-4-phenylpyridinium-induced H2O2 production and death in mesencephalic dopaminergic and cortical neurons. In the absence of 1-methyl-4-phenylpyridinium, the fibroblast growth factor 9-induced H2O2 reduction is blocked by HO-1 inhibitors, but not by gamma-GCS inhibitors
physiological function
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expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent
physiological function
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expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent
physiological function
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expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent
physiological function
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gamma-GCS is rate-limiting catalyzing the regulated step of GSH biosynthesis, being both transcriptionally and post-translationally regulated, post-translational regulation of the gamma-GCS enzyme by the redox environment
physiological function
glutathione biosynthesis catalysed by glutamate-cysteine ligase and glutathione synthetase, EC 6.3.2.3, is essential for maintaining redox homoeostasis and protection against oxidative damage in diverse eukaroytes and bacteria
physiological function
GSH is an essential thiol antioxidant produced in the cytosol of all cells and plays a key role in protecting against oxidative stress by neutralising free radicals and reactive oxygen species (ROS). The decline in GSH has been associated with changes in the expression and activity of the rate-limiting enzyme glutamate cysteine ligase (GCL), which produces the intermediate dipeptide gamma-glutamylcysteine. The molecular mechanisms that affect these age-related changes and the complexity of GCL regulation are analyzed. Impairment of the transcriptional activity of Nrf2 contributes to GCL dysregulation in aged rats
physiological function
GSH is synthesized de novo in a two-step process catalyzed by glutamate cysteine ligase (GCL, EC 6.3.2.2), and glutathione synthetase (GS, EC 6.3.2.3). GCL catalyzes the first and rate-limiting step, in which glutamate is ligated with cysteine to form gamma-glutamylcysteine (gamma-GC), which is rapidly linked to glycine to form GSH via the action of glutathione synthetase. Increased expression and enzymatic activity of enzyme GCL is closely associated with renal cell carcinoma (RCC) suggesting an important role for glutathione in the pathogenesis of RCC
physiological function
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the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS)
physiological function
C1KBE8; C1KBE7;
the enzyme catalyses the synthesis of gamma-glutamylcysteine, a precursor of glutathione (GSH). GSH is an important intracellular molecule that protects cells against endogenous and exogenous oxidative stress, and plays a critical role in maintaining cellular redox homeostasis
physiological function
P97494; O09172;
glutathione (GSH) is synthesized by a two-step enzyme reaction. In the first step, L-cysteine is ligated to the gamma carboxyl group of L-glutamic acid by glutamate-cysteine-ligase (GCL, EC 6.3.2.2), and in the second step L-glycine is bound to gamma-glutamylcysteine by glutathione synthase (EC 6.3.2.3). The first step is the ratelimiting step. Compared with the holoenzyme, the catalytic GCLc monomer shows lower enzymatic activity but higher sensitivity to feedback inhibition by GSH. Involvement of GCL activity in the increase in the intracellular GSH level induced by beta-carotene
physiological function
the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 activity; the enzyme is required for biosynthesis of glutathione. Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics
physiological function
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gamma-glutamylcysteine synthetase (gamma-ECS) is a key enzyme in the biosynthesis pathway of glutathione (GSH), the precursor of phytochelatins. The overexpression of the bacterial gamma-glutamylcysteine synthetase in Populus tremula x Populus alba mediates changes in cadmium influx, allocation and detoxification in poplar, analysis of net Cd2+ influx in association with H+/Ca2+, Cd tolerance, and the underlying molecular and physiological mechanisms, overview. GSH-mediated induction of the transcription of genes involved in Cd2+ transport and detoxification
physiological function
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the enzyme catalyzes the first rate-limiting step in the biosynthesis of glutathione. Glutathione (GSH) is the keystone of the cellular response toward oxidative stress. Elevated GSH content correlates with increased resistance to chemotherapy and radiotherapy of head and neck (HN) tumors. Nuclear localization of glutamate-cysteine ligase is associated with proliferation in head and neck squamous cell carcinoma. The localization of GSH synthesis contributes to the protection against oxidative stress within hotspots of cell proliferation. The expression of glutamate-cysteine ligase (GCL) accounts for the increased GSH availability observed in head and neck squamous cell carcinoma (SCC). No role of the NRF2 and NF?kappaB signaling pathways in GCLM activation
physiological function
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expression of both glutamate-cysteine ligase catalytic and modifier subunit is mediated by the GCN2/ATF4 stress response pathway. Regulation of modifier subunit GCLM expression may be mediated by changes in the abundance of mRNA stabilizing or destabilizing proteins. Upregulation of GCLM levels in response to low cysteine levels may serve to protect the cell in the face of a future stress requiring GSH as an antioxidant or conjugating/detoxifying agent
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physiological function
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the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 activity; the enzyme is required for biosynthesis of glutathione. Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics
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physiological function
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the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS)
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additional information
MALDI-TOF mass spectrometric analysis of tryptic peptides, mapping of the identify the cysteinyl residue target of the S-glutathionylation reaction, which occurs at the Cys residue at position 386. Three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
additional information
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GCL is a heterodimeric enzyme, consisting of a catalytic subunit, (GCLc) and a modulatory subunit (GCLm) that are encoded by two distinct genes. GCLc constitutes all the enzymatic activity, but catalytic efficiency is increased substantially by covalent interaction with GCLm
additional information
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positive interaction between two subunits of glutamate-cysteine ligase is detected using the yeast two-hybrid system. Enzyme protein structure prediction using the glutamate-cysteine ligase in complex with Mg2+ and L-glutamate, comparisons of tertiary structures, overview
additional information
C1KBE8; C1KBE7;
positive interaction between two subunits of glutamate-cysteine ligase is detected using the yeast two-hybrid system. Enzyme protein structure prediction using the glutamate-cysteine ligase in complex with Mg2+ and L-glutamate, comparisons of tertiary structures, overview
additional information
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MALDI-TOF mass spectrometric analysis of tryptic peptides, mapping of the identify the cysteinyl residue target of the S-glutathionylation reaction, which occurs at the Cys residue at position 386. Three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-ethyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-ethyl-L-glutamyl-L-alpha-aminobutyrate
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ir
ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
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ir
ATP + alpha-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-L-glutamyl-L-alpha-aminobutyrate
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ir
ATP + alpha-methylglutamate + L-Cys
ADP + phosphate + alpha-methylglutamyl-L-Cys
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i.e. 2-amino-2-methylpentanedioate
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ATP + beta-aminoglutarate + L-Cys
ADP + phosphate + beta-aminoglutaryl-L-Cys
-
i.e. 3-aminopentanedioate
-
-
-
ATP + beta-Glu + L-Cys
ADP + phosphate + beta-Glu-L-Cys
-
17.6% of the activity relative to L-Glu
-
-
-
ATP + beta-glutamate + L-alpha-aminobutyrate
ADP + phosphate + beta-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + beta-methyl-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + beta-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + beta-methylglutamate + L-Cys
ADP + phosphate + beta-methylglutamyl-L-Cys
-
i.e. 2-amino-3-methylpentanedioate
-
-
-
ATP + DL-alpha-aminoadipate + L-cysteine
ADP + phosphate + DL-aminoadipyl-L-cysteine
-
about 10% of the activity with L-glutamate
-
-
?
ATP + DL-alpha-aminomethylglutarate + L-alpha-aminobutyrate
ADP + phosphate + DL-alpha-aminomethylglutaryl-L-alpha-aminobutyrate
-
-
ir
ATP + DL-alpha-aminomethylsuccinate + L-alpha-aminobutyrate
ADP + phosphate + DL-alpha-aminomethylsuccinyl-L-alpha-aminobutyrate
-
-
ir
ATP + DL-beta-aminoadipate + L-alpha-aminobutyrate
ADP + phosphate + DL-beta-aminoadipyl-L-alpha-aminobutyrate
-
-
ir
ATP + glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
random ter-reactant mechanism with a preferred binding order
-
-
?
ATP + L-Glu + (R)-beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-(R)-beta-amino-iso-butyrate
-
2fold less reactive as the S-isomer
-
ir
ATP + L-Glu + (S)-beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-(S)-beta-amino-iso-butyrate
-
2fold as reactive as the R-isomer
-
ir
ATP + L-Glu + allo-L-threonine
ADP + phosphate + gamma-L-Glu-allo-L-threonine
-
-
ir
ATP + L-Glu + beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-beta-amino-iso-butyrate
-
-
ir
ATP + L-Glu + beta-cyano-L-alanine
ADP + phosphate + gamma-L-Glu-beta-cyano-L-alanine
-
-
ir
ATP + L-Glu + DL-beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
-
ir
ATP + L-Glu + gamma-aminobutyrate
ADP + phosphate + gamma-L-Glu-gamma-aminobutyrate
-
mutant R366A
-
r
ATP + L-Glu + gamma-aminobutyrate
ADP + phosphate + L-Glu-gamma-aminobutyrate
-
-
-
ir
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-L-Glu-hydroxylamine
-
slow reaction rate
-
-
ATP + L-Glu + L-2-aminobutyrate
ADP + phosphate + gamma-L-Glu-2-aminobutyrate
-
-
-
?
ATP + L-Glu + L-alpha-aminoheptanoate
ADP + phosphate + gamma-L-Glu-L-alpha-aminoheptanoate
-
-
ir
ATP + L-Glu + L-C-allylglycine
ADP + phosphate + gamma-L-Glu-L-C-allylglycine
-
-
ir
ATP + L-Glu + L-isoleucine
ADP + phosphate + gamma-L-Glu-L-isoleucine
-
-
ir
ATP + L-Glu + L-leucine
ADP + phosphate + gamma-L-Glu-L-leucine
-
-
ir
ATP + L-Glu + L-valine
ADP + phosphate + gamma-L-Glu-L-valine
-
-
ir
ATP + L-Glu + n-propylamine
ADP + phosphate + N-propyl-L-glutamine
-
-
-
-
?
ATP + L-Glu + O-methyl-DL-serine
ADP + phosphate + gamma-L-Glu-O-methyl-DL-serine
-
-
ir
ATP + L-Glu + S-methyl-L-Cys
ADP + phosphate + gamma-L-Glu-L-S-methyl-Cys
-
-
ir
ATP + L-Glu + S-methyl-L-cysteine
ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
-
ir
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
ATP + N-methyl-L-glutarate + L-Cys
ADP + phosphate + N-methyl-L-glutaryl-L-Cys
-
-
-
-
-
ATP + threo-beta-hydroxy-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + threo-beta-hydroxy-DL-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + threo-beta-hydroxy-L-Glu + L-Cys
ADP + phosphate + threo-beta-hydroxy-L-Glu-L-Cys
-
-
-
-
-
ATP + threo-gamma-hydroxy-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + threo-gamma-hydroxy-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
glutamate + ATP + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
assay at pH 8.2
-
-
?
GTP + L-Glu + L-Cys
GDP + phosphate + gamma-L-Glu-L-Cys
-
87% of the activity relative to ATP
-
-
-
L-glutamate + L-cysteine + ATP
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
UTP + L-Glu + L-Cys
UDP + phosphate + gamma-L-Glu-L-Cys
-
12% of the activity relative to ATP
-
-
-
ATP + D-Glu + L-2-aminobutyrate
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
-
-
?
ATP + D-Glu + L-2-aminobutyrate
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
-
-
-
?
ATP + D-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
-
ir
ATP + D-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
-
ir
ATP + D-Glu + L-Cys
ADP + phosphate + D-Glu-L-Cys
-
8.5% of the activity relative to L-Glu
-
-
-
ATP + L-Glu + beta-chloro-L-Ala
ADP + phosphate + gamma-L-Glu-L-beta-chloro-L-Ala
-
reaction sequence: L-Glu binding, ATP binding, ADP release, L-beta-chloroalanine binding, phosphate release, dipeptide release
-
-
-
ATP + L-Glu + beta-chloro-L-Ala
ADP + phosphate + gamma-L-Glu-L-beta-chloro-L-Ala
-
strain KM: 79% of the activity relative to L-Cys, strain W: 99% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + beta-chloro-L-Ala
ADP + phosphate + gamma-L-Glu-L-beta-chloro-L-Ala
-
-
-
-
-
ATP + L-Glu + beta-chloro-L-alanine
ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
-
ir
ATP + L-Glu + beta-chloro-L-alanine
ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
-
ir
ATP + L-Glu + DL-allylglycine
ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
-
-
-
-
ATP + L-Glu + DL-allylglycine
ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
-
ir
ATP + L-Glu + Gly
ADP + phosphate + gamma-L-Glu-Gly
-
-
ir
ATP + L-Glu + Gly
ADP + phosphate + gamma-L-Glu-Gly
-
14.5% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + Gly
ADP + phosphate + gamma-L-Glu-Gly
-
-
ir
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
strain KM: 85% of the activity relative to L-Cys, strain W: 81% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
Escherichia coli B / ATCC 11303
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
60% of the activity relative to L-Cys
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
-
ATP + L-Glu + L-2-aminobutyrate
ADP + phosphate + L-Glu-2-aminobutyrate
-
-
-
?
ATP + L-Glu + L-2-aminobutyrate
ADP + phosphate + L-Glu-2-aminobutyrate
-
-
-
?
ATP + L-Glu + L-2-aminobutyrate
ADP + phosphate + L-Glu-2-aminobutyrate
-
-
-
?
ATP + L-Glu + L-Ala
ADP + phosphate + gamma-L-Glu-L-Ala
-
10.9% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-alanine
ADP + phosphate + gamma-L-Glu-L-alanine
-
-
ir
ATP + L-Glu + L-alanine
ADP + phosphate + gamma-L-Glu-L-alanine
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
?
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
?
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
ir
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
-
-
r
ATP + L-Glu + L-Cys
?
-
enzyme catalyzes the first committed step in the biosynthesis of trypanothione, i.e. diglutathionylspermidine
-
-
-
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
the enzyme has key influence on glutathione homeostasis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
-
-
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
catalyzes the biosynthesis of the GSH precursor
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate-limiting step in the biosynthesis of glutathione
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
first and rate-limiting step in the GSH biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Escherichia coli B / ATCC 11303
-
catalyzes the biosynthesis of the GSH precursor
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
first and rate-limiting step in the GSH biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
combines glutamate and cysteine through the gamma carboxylmoiety rather than the alpha carboxyl moiety found in protein amide bonds, imparting resistance to proteolytic degradation
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
reaction can be performed by the catalytic subunit alone, but presence of the regulatory subunit in the holoenzyme increases the activity
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate limiting step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate limiting step in GSH biosynthesis, rare hereditary enzyme deficiency is associated with low erythrocyte levels of the enzyme leading to hemolytic anemia
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate-limiting step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate-limiting step in glutathione biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting enzyme in the GSH biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis, regulation mechanism and model
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
regulation and signaling in GSH de novo synthesis pathway
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate-limiting step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P97494;, Q97SC0;
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
r
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
first and rate-limiting step in the glutathione biosynthesis, important for maintenance of the intracellular thiol redox status and in detoxification processes
-
r
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
the enzyme is involved in the biosynthesis of GSH, which is used for detoxification of herbicides by the plant
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
1121, 1122, 1123, 1124, 1125, 1129, 1130, 1132, 1133, 1134, 1135, 1136, 1138, 1139, 1144, 1147, 1150
-
-
-
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate limiting step in GSH de novo biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first step in glutathione biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
part of GSH biosynthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step of the chemoprotective glutathione synthesis
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first step in the biosynthesis of trypanothione via GSH
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first step in the de novo biosynthesis of the tripeptide glutathione
-
r
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-homocysteine
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
13.7% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-homocysteine
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
-
-
-
-
ATP + L-Glu + L-homocysteine
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
-
ir
ATP + L-Glu + L-homoserine
ADP + phosphate + gamma-L-Glu-L-homoserine
-
17% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-homoserine
ADP + phosphate + gamma-L-Glu-L-homoserine
-
-
ir
ATP + L-Glu + L-norleucine
ADP + phosphate + gamma-L-Glu-L-norleucine
-
-
ir
ATP + L-Glu + L-norleucine
ADP + phosphate + gamma-L-Glu-L-norleucine
-
-
ir
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
ir
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
ir
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
14% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
-
-
-
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
ir
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
strain KM: 18% of the activity relative to L-Cys, strain W: 13% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
14.5% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + L-serine
ADP + phosphate + gamma-L-Glu-L-serine
-
-
ir
ATP + L-Glu + L-serine
ADP + phosphate + gamma-L-Glu-L-serine
-
-
ir
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
-
allo-L-threonine is a 5fold better substrate than L-threonine
-
ir
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
-
-
ir
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
-
-
ir
ATP + L-Glu + S-methyl-L-Cys
ADP + phosphate + gamma-L-Glu-S-methyl-L-Cys
-
strain KM: 70% of the activity relative to L-Cys, strain W: 70% of the activity relative to L-Cys
-
-
-
ATP + L-Glu + S-methyl-L-Cys
ADP + phosphate + gamma-L-Glu-S-methyl-L-Cys
-
-
-
-
-
ATP + L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-(2-aminobutyrate)
2-aminobutyrate can replace cysteine, although with a lower activity
-
-
?
ATP + L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-(2-aminobutyrate)
2-aminobutyrate can replace cysteine, although with a lower activity
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
D4N892;
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Actinobacillus pleuropneumoniae ATCC 55618
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
redox regulation of the enzyme, overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
C1KBE8; C1KBE7;
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
the enzyme plays a role in disease resistance in Arabidopsis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
the thiol-based regulation of glutamate-cysteine ligase provides a posttranslational mechanism for modulating enzyme activity in response to in vivo redox environment
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione biosynthesis, plays a central role in glutathione homeostasis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
rate-limiting step in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
rate-limiting enzyme in glutathione synthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
overexpression of gamma-GCS decreases drug-induced oxidative stress and confers drug resistance
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
treatment of human breast cancer cells with 2-deoxy-D-glucose causes metabolic oxidative stress that is accompanied by increases in steady-state levels of glutamate cysteine ligase mRNA, glutamate cysteine ligase activity and glutathione content
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
upregulation of gamma-glutamate-cysteine ligase is part of the long-term adaptation process to iron accumulation in neuronal SH-SY5Y cells
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
evidence of TNF-alpha-mediated LEDGF induction of gamma-glutamylcysteine synthetase heavy subunit and mRNA expression. TNF-alpha-induced intracellular level of reactive oxygen species is critical for the regulation of the multidomain adaptor protein LEDGF, which subsequently influences cellular glutathione content by regulating transcription of gamma-glutamylcysteine synthetase heavy subunit
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first rate-limiting step in GSH biosynthesis, GCL is a major determinant of cellular GSH levels, pathway overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL is the key glutathione-synthesizing enzyme
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL is the rate-limiting enzyme in glutathione biosynthesis, its catalytic subunit GCLC determines this de novo synthesis. Induction of GCLC is a strategy to enhance the antioxidant capability in cells
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione synthesis, a mutation in the catalytic subunit gene 5'-UTR leads to reduced enzyme activity
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
the enzyme acts endogenously as an antioxidant and is involved in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL-mediated phosphorylation of L-glutamate creating the activated enzyme-bound gamma-glutamylphosphate intermediate
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P97494; O09172;
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first step in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in GSH synthesis. Overexpression of the catalytic and modifier subunits of the enzyme leads to enhanced GCL activity and resistance to TNF-induced apoptosis. Maintenance of mitochondrial integrity is a major mechanism of protection against TNF-induced apoptosis in Hepa-1 cells overexpressing the enzyme
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in the glutathione biosynthesis pathway
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
the mechanism of modulation of eukaryotic gamma-glutamylcysteine ligase enzymes may include specific binding of ligands such as pyridine dinucleotide phosphates and reversible protein phosphorylation
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first rate-limiting step in GSH biosynthesis, GCL is a major determinant of cellular GSH levels, pathway overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL-mediated phosphorylation of L-glutamate creating the activated enzyme-bound gamma-glutamylphosphate intermediate
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first step of glutathione synthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
gonadotropins regulate expression of follicular glutamate cysteine ligase in a follicle stage-dependent manner and in a glutamate cysteine ligase subunit-dependent manner
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione synthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in GSH synthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
thyroid hormone promotes glutathione synthesis in astrocytes by upregulation of glutamate cysteine ligase through differential stimulation of its catalytic and modulator subunit mRNAs
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first rate-limiting step in GSH biosynthesis, GCL is a major determinant of cellular GSH levels, pathway overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
mechanisms in regulation of GCLC and GCLM expression, overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL-mediated phosphorylation of L-glutamate creating the activated enzyme-bound gamma-glutamylphosphate intermediate
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
assay at pH 8
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
reaction is catalyzed by the bifunctional enzyme gamma-glutamylcysteine synthetase-glutathione synthetase
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Streptococcus agalactiae serotype V
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Streptococcus agalactiae serotype V ATCC BAA-611 / 2603 V/R
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
first step in the biosynthesis of glutathione, pathway overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
redox regulation of the enzyme, overview
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
chilling stress strongly induces gamm-ECS mRNA
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
additional information
?
-
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview
-
-
-
additional information
?
-
-
substrate specificity, beta-alanine, (R,S)-beta-amino-n-butyrate, and (R,S)-alpha-ethyl-beta-alanine are no substrates
-
?
additional information
?
-
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. CC2 plays a role in GCL redox regulation, overview
-
-
-
additional information
?
-
-
enhancement of the glutathione biosynthetic capability, particularly in neuronal tissues, can extend the life span of flies
-
-
-
additional information
?
-
substrate specificity, poor substrates are beta-glutamate, (R,S)-beta-methyl-DL-glutamate, (R,S)-gamma-methyl-glutamate, L-aspartate, and DL-alpha-aminoadipate
-
?
additional information
?
-
-
enzyme is able to to combine glutamine and amines to form gamma-glutamylamides. The reaction rate depende on the length if the methylene chain of the amines in the following decreasing order: n-propylamine > butylamine > ethylamine > methylamine
-
-
-
additional information
?
-
substrate specificity, poor substrates are beta-glutamate, (R,S)-beta-methyl-DL-glutamate, (R,S)-gamma-methyl-glutamate, L-aspartate, and DL-alpha-aminoadipate
-
?
additional information
?
-
hyperthermal stress triggers adaptive increases in intracellular GSH biosynthesis in cnidarians as a protective response to oxidative/nitrosative stress, overview
-
-
-
additional information
?
-
-
hyperthermal stress triggers adaptive increases in intracellular GSH biosynthesis in cnidarians as a protective response to oxidative/nitrosative stress, overview
-
-
-
additional information
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, enzyme overexpression provides resistance to melphalan and other drugs, overview, protection of cancer cells by increased GSH levels
-
?
additional information
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, enzyme overexpression provides resistance to melphalan and other drugs, overview, protection of cancer cells by increased GSH levels
-
?
additional information
?
-
-
overexpression of cytochrome P450 2E1 in human hepatocarcinoma cell line HepG2 increases the intracellular H2O2 level by 40-50% and therefore results in a 2fold increase in enzyme expression
-
?
additional information
?
-
-
the genotype of GLCLC is associated with drug sensitivity or resistance, respectively
-
?
additional information
?
-
-
GCL activity is not associated with susceptibility to chronic obstructive pulmonary disease patients or disease severity, overview
-
-
-
additional information
?
-
-
GCLC polymorphisms are associated with lower lung function levels causing lung disease, especially in association with oxidative stress due to smoking
-
-
-
additional information
?
-
-
insulin stimulation of GCL catalytic subunit expression increases endothelial GSH during oxidative stress, overview. Functional importance of insulin in Nrf2-dependent transcriptional upregulation of GCLC in GSH recovery during oxidative challenge, role for Nrf2 involvement in both constitutive and inducible endothelial GCLc expression and GSH synthesis, while PI3K/Akt/mTOR signaling appears to participate only in insulin-inducible GSH synthesis. Low glucose enhances the insulin-mediated increase in GCLc expression
-
-
-
additional information
?
-
-
post-translational regulation of GCL, overview. GCLC and GCLM polymorphisms increase disease susceptibility in humans, overview
-
-
-
additional information
?
-
-
the cis-element signaling of Nrf2/EpRE is involved in resveratrol-mediated induction of GCL genes
-
-
-
additional information
?
-
-
the modifier subunit GCLM is not correlated with methamphetamine-use disorder or schizophrenia in the Japanese population, overview
-
-
-
additional information
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
Q97SC0;
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
-
ARE-driven gene expression of Gclc via a MEK/Nrf2 pathway can help to protect macrophages from oxidative stress due to hyperhomocysteinemia
-
-
-
additional information
?
-
-
post-translational regulation of GCL, overview
-
-
-
additional information
?
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays a role in GCL redox regulation, overview
-
-
-
additional information
?
-
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
the enzyme forms gamma-glutamyl-Tris in Tris buffers, substrate specificity, the L-glutamate analogues L-alpha-aminoadipate, L-asparate, glutarate, gamma-aminobutyrate, and gamma-methyl-DL-glutamate are poor substrates, beta-alanine, RS-beta-amino-n-butyrate, and RS-alpha-ethyl-beta-alanine are no substrates
-
?
additional information
?
-
the enzyme forms gamma-glutamyl-Tris in Tris buffers, substrate specificity, the L-glutamate analogues L-alpha-aminoadipate, L-asparate, glutarate, gamma-aminobutyrate, and gamma-methyl-DL-glutamate are poor substrates, beta-alanine, RS-beta-amino-n-butyrate, and RS-alpha-ethyl-beta-alanine are no substrates
-
?
additional information
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
-
?
additional information
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
-
?
additional information
?
-
-
differential regulation of glutamate-cysteine ligase subunit expression and increased holoenzyme formation in response to cysteine deprivation
-
-
-
additional information
?
-
-
induced acute edematous pancreatitis is characterized by marked glutathione depletion in the pancreas, and a rapid restoration of GSH levels involving the enzyme, overview
-
-
-
additional information
?
-
-
post-translational regulation of GCL, overview
-
-
-
additional information
?
-
tumor development in gut tissue does not affect GCS enzyme activity
-
-
-
additional information
?
-
-
tumor development in gut tissue does not affect GCS enzyme activity
-
-
-
additional information
?
-
-
purified rat kidney GCL holoenzyme is capable of undergoing autophosphorylation, the phosphorylation is specific for the GCLC subunit, no phosphorylation of the GCLM subunit
-
-
-
additional information
?
-
-
Met4 regulates the GSH1 expression in response to GSH availability, model for genetic regulation and control of GSH biosynthesis
-
?
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
additional information
?
-
the bifunctiona enzyme also catalyzes the reaction of EC 6.3.2.3, gltathione synthetase
-
-
-
additional information
?
-
the bifunctiona enzyme also catalyzes the reaction of EC 6.3.2.3, gltathione synthetase
-
-
-
additional information
?
-
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
-
additional information
?
-
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
-
binding of ATP to the enzyme increases the binding affinity for L-Glu by 18fold, while binding of L-Glu or L-alpha-aminobutyrate decreases the affinity for binding of the other by 6fold
-
?
additional information
?
-
most of the GSH produced in this pathway is converted to trypanothione
-
?
additional information
?
-
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-Glu + L-Cys
?
-
enzyme catalyzes the first committed step in the biosynthesis of trypanothione, i.e. diglutathionylspermidine
-
-
-
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Q56277
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P46309
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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the enzyme has key influence on glutathione homeostasis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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catalyzes the biosynthesis of the GSH precursor
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate-limiting step in the biosynthesis of glutathione
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P0A6W9
first and rate-limiting step in the GSH biosynthesis
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P0A6W9
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Escherichia coli B / ATCC 11303
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catalyzes the biosynthesis of the GSH precursor
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P0A6W9
first and rate-limiting step in the GSH biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate limiting step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate limiting step in GSH biosynthesis, rare hereditary enzyme deficiency is associated with low erythrocyte levels of the enzyme leading to hemolytic anemia
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate-limiting step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate-limiting step in glutathione biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P48506, P48507
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting enzyme in the GSH biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step in glutathione biosynthesis, regulation mechanism and model
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
regulation and signaling in GSH de novo synthesis pathway
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P90557
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first and rate-limiting step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P97494, Q97SC0
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Q9NFN6
first and rate-limiting step in the glutathione biosynthesis, important for maintenance of the intracellular thiol redox status and in detoxification processes
-
r
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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the enzyme is involved in the biosynthesis of GSH, which is used for detoxification of herbicides by the plant
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first and rate limiting step in GSH de novo biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
first step in glutathione biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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part of GSH biosynthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P19468, P48508
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step of the chemoprotective glutathione synthesis
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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-
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
P32477
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate-limiting step in glutathione biosynthesis, regulation mechanism
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Q09768
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first step in the biosynthesis of trypanothione via GSH
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?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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first step in the de novo biosynthesis of the tripeptide glutathione
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r
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate limiting and first step in glutathione biosynthesis
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
Q26820
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
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ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
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rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
D4N892
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Actinobacillus pleuropneumoniae ATCC 55618
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
A6VQP8
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
A6VQP8
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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redox regulation of the enzyme, overview
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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rate-limiting enzyme in glutathione biosynthesis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
C1KBE8 AND C1KBE7
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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the enzyme plays a role in disease resistance in Arabidopsis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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the thiol-based regulation of glutamate-cysteine ligase provides a posttranslational mechanism for modulating enzyme activity in response to in vivo redox environment
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
O23736
rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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rate-limiting enzyme in glutathione biosynthesis, plays a central role in glutathione homeostasis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
B2ZG39
rate-limiting step in glutathione biosynthesis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P48506 AND P48507
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P48506 AND P48507
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P48506
rate-limiting enzyme in glutathione synthesis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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overexpression of gamma-GCS decreases drug-induced oxidative stress and confers drug resistance
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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treatment of human breast cancer cells with 2-deoxy-D-glucose causes metabolic oxidative stress that is accompanied by increases in steady-state levels of glutamate cysteine ligase mRNA, glutamate cysteine ligase activity and glutathione content
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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upregulation of gamma-glutamate-cysteine ligase is part of the long-term adaptation process to iron accumulation in neuronal SH-SY5Y cells
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first rate-limiting step in GSH biosynthesis, GCL is a major determinant of cellular GSH levels, pathway overview
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
GCL is the key glutathione-synthesizing enzyme
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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GCL is the rate-limiting enzyme in glutathione biosynthesis, its catalytic subunit GCLC determines this de novo synthesis. Induction of GCLC is a strategy to enhance the antioxidant capability in cells
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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rate-limiting enzyme in glutathione synthesis, a mutation in the catalytic subunit gene 5'-UTR leads to reduced enzyme activity
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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the enzyme acts endogenously as an antioxidant and is involved in glutathione biosynthesis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P97494 AND O09172
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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first step in glutathione biosynthesis
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in GSH synthesis. Overexpression of the catalytic and modifier subunits of the enzyme leads to enhanced GCL activity and resistance to TNF-induced apoptosis. Maintenance of mitochondrial integrity is a major mechanism of protection against TNF-induced apoptosis in Hepa-1 cells overexpressing the enzyme
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in the glutathione biosynthesis pathway
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P97494
the mechanism of modulation of eukaryotic gamma-glutamylcysteine ligase enzymes may include specific binding of ligands such as pyridine dinucleotide phosphates and reversible protein phosphorylation
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first rate-limiting step in GSH biosynthesis, GCL is a major determinant of cellular GSH levels, pathway overview
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
rate-limiting enzyme in glutathione biosynthesis
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Q1W2L8
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
first step of glutathione synthesis
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Q3IEB7
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Q3IEB7
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-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P19468
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?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
P19468
gonadotropins regulate expression of follicular glutamate cysteine ligase in a follicle stage-dependent manner and in a glutamate cysteine ligase subunit-dependent manner
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?