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ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
-
ir
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 + 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 + 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 + L-Glu
ADP + phosphate + 5-oxoproline
-
-
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
-
-
ir
ATP + L-Glu + DL-beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
-
ir
ATP + L-Glu + Gly
ADP + phosphate + gamma-L-Glu-Gly
-
-
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-aminoheptanoate
ADP + phosphate + gamma-L-Glu-L-alpha-aminoheptanoate
-
-
ir
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
ir
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
-
-
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-serine
ADP + phosphate + gamma-L-Glu-L-serine
-
-
ir
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
-
-
ir
ATP + L-Glu + S-methyl-L-cysteine
ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
-
ir
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + threo-beta-hydroxy-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + threo-beta-hydroxy-DL-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + threo-gamma-hydroxy-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + threo-gamma-hydroxy-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + alpha-methyl-L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate
-
-
-
-
?
ATP + alpha-methylglutamate + L-Cys
ADP + phosphate + alpha-methylglutamyl-L-Cys
-
i.e. 2-amino-2-methylpentanedioate
-
-
?
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-methylglutamate + L-Cys
ADP + phosphate + beta-methylglutamyl-L-Cys
-
i.e. 2-amino-3-methylpentanedioate
-
-
?
ATP + D-Glu + L-Cys
ADP + phosphate + D-Glu-L-Cys
-
-
-
?
ATP + L-Glu + beta-chloro-L-Ala
ADP + phosphate + gamma-L-Glu-L-beta-chloro-L-Ala
-
-
-
-
?
ATP + L-Glu + DL-allylglycine
ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
-
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-L-Glu-hydroxylamine
-
slow reaction rate
-
?
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
-
?
ATP + L-Glu + L-Ala
ADP + phosphate + gamma-L-Glu-L-Ala
-
-
-
-
?
ATP + L-Glu + L-Cys
?
-
glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
ATP + L-Glu + L-homocysteine
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
-
-
-
?
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
-
-
?
ATP + L-Glu + L-Thr
ADP + phosphate + gamma-L-Glu-L-Thr
-
-
-
-
?
ATP + L-Glu + S-methyl-L-Cys
ADP + phosphate + gamma-L-Glu-S-methyl-L-Cys
-
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
ATP + N-methyl-L-glutarate + L-Cys
ADP + phosphate + N-methyl-L-glutaryl-L-Cys
-
-
-
-
?
ATP + threo-beta-hydroxy-L-Glu + L-Cys
ADP + phosphate + threo-beta-hydroxy-L-Glu-L-Cys
-
-
-
-
?
additional information
?
-
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
assay at pH 8
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
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
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
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
-
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-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 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
-
-
?
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
-
-
?
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ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
ATP + L-Glu + L-Cys
?
-
glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
ATP + L-glutamate + L-cysteine
ADP + phosphate + L-glutamyl-L-cysteine
-
-
-
-
?
additional information
?
-
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-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-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 GSH synthesis
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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4-methylene-L-glutamate
weak, competitive
5-Chloro-4-oxo-L-norvaline
irreversible, binding is reduced by L-glutamate, increased by L-alpha-aminobutyrate, and is completely dependent on divalent cations
cysteamine
rapid inactivation, reversible by thiols
D-3-amino-1-chloro-2-pentanone
-
gamma-methylene-D-glutamate
-
L-buthionine sulfone
competitive, reversible
L-buthionine-R-sulfoximine
mechanism-based, competitive, reversible
L-buthionine-S-sulfoximine
L-glutamine
inhibition of enzyme activity in tumor tissue
methionine sulfoximine
competitive and reversible
S-butyl-DL-homocysteine-SR-sulfoximine
-
S-nitroso-L-cysteine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
S-nitroso-L-cysteinylglycine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
Trinitrobenzene sulfonate
inactivates the enzyme
4-Methylene glutamate
-
-
4-methylene-L-glutamate
-
5-Chloro-4-oxo-L-norvaline
-
alpha-Methyl-DL-glutamate
-
-
ciprofibrate
-
inhibits expression of heavy subunit
cis-1-Amino-1,3-dicarboxycyclohexane
-
-
D-3-amino-1-chloro-2-pentanone
-
highly potent irreversible inactivator
diquat
-
inhibits expression of heavy subunit
DL-2-Amino-4-phosphonobutanoate
-
-
DL-alpha-Aminomethylglutarate
-
-
gamma-Glu-2-aminobutanoyl-Gly
-
i.e. ophthalmic acid, inhibits only slightly, but inhibits much more after treatment of the holoenzyme with DTT, the recombinant and isolated heavy subunit enzyme is substantially inhibited without DTT
L-2-Amino-4-oxo-5-chloropentanoate
-
inactivation requires very low concentration, 0.003-0.006 mM, of Mg2+ or certain other divalent cations, L-Glu, but not D-Glu protects competitively against inactivation, protection is increased in the presence of ATP or ADP
L-2-aminohexanedioate
-
i.e. L-alpha-aminoadipate
L-3-Amino-1-chloro-2-pentanone
-
highly potent irreversible inactivator
L-buthionine-(S,R)-sulfoximine
-
cotreatment with L-buthionine-(S,R)-sulfoximine, 1-methyl-4-phenylpyridinium and fibroblast growth factor 9 inhibits increased neuron viability compared to the group treated with 1-methyl-4-phenylpyridinium and fibroblast growth factor 9, to levels comparable to those of the 1-methyl-4-phenylpyridinium-treated group
L-buthionine-S-sulfoximine
-
specific inhibitor
L-buthionine-SR-sulfoximine
-
specific
L-cysteine
-
varying glutamic acid concentrations from 5 to 80 mM do not affect GCL activities markedly, whereas cysteine concentrations from 2.5 to 40 mM influence GCL activities substantially in a tissue-dependent manner, about 20 mM L-Cys is optimal in the different tissue, overview. Low doses activate high doses inhibits the enzyme
L-Homocysteine sulfinate
-
-
L-methionine
-
inhibits expression of heavy subunit
lipopolysaccharides
-
inhibits expression of heavy subunit
-
N-[2(2-Aminoethyl)-dithioethyl]4-azido-2-nitrobenzeneamine
-
-
S-(S-Methyl)cysteamine
-
-
threo-beta-Hydroxy-DL-glutamate
-
-
threo-gamma-Hydroxy-L-glutamate
-
-
trans-1-Amino-1,3-dicarboxycyclohexane
-
-
Trinitrobenzene sulfonate
-
addition of 10 mM Mg2+ results in a 16fold increase of inactivation rate, Lys-38 in the heavy subunit is significantly modified in presence of Mg2+
GSH
-
-
GSH
feedback inhibition, competitive to L-Glu
L-buthionine-S-sulfoximine
-
-
L-buthionine-S-sulfoximine
mechanism-based, ATP-dependent, nearly irreversible inhibition in presence of Mg2+ and ATP, if ATP and Mg2+ are remove the activity is restored
buthionine sulfoximine
-
-
buthionine sulfoximine
-
inhibition is about 20times more effectively than with prothionine sulfoximine, and at least 100times more effective than methionine sulfoximine
buthionine sulfoximine
-
GCL mediates the phosphorylation of buthionine sulfoximine, which is required for its tight and irreversible binding to the active site of GCL
cystamine
-
-
cystamine
-
L-Glu protects, ATP enhances rate of inactivation
cystamine
-
completely reversible by DTT
cystamine
-
7.5 mM MgCl2 + 7.5 mM L-Glu protect
gamma-Methylglutamate
-
-
gamma-Methylglutamate
-
D-isomer inhibits, L-isomer not, competitively towards Glu, inactivation is dependent upon the presence of Mg2+ or Mn2+, Glu protects against inactivation
glutathione
-
-
glutathione
-
feed-back inhibition
glutathione
-
inhibited by both GSSG and GSH
glutathione
-
whole enzyme and large subunit inhibited
glutathione
-
feedback inhibition, subunit GCLM increases the Ki for GSH-mediated feedback inhibition of GCL, competitive to glutamate
GSH
-
-
GSH
-
feedback inhibition, acts on the heavy catalytic subunit
methionine sulfoximine
-
-
methionine sulfoximine
-
of the 4 stereoisomers only L-methionine-S-sulfoximine inhibits
methionine sulfoximine
-
and analogs, no effect on glutamine synthetase
Prothionine sulfoximine
-
-
Prothionine sulfoximine
-
no effect on glutamine synthetase
Prothionine sulfoximine
-
i.e. S-n-propyl homocysteine sulfoximine
S-sulfocysteine
-
-
S-sulfocysteine
-
D-enantiomer and L-enantiomer, ATP is not required for inactivation, noncovalent binding of close to 1 mol of inactivator per mol of enzyme, competitive with respect to L-Glu, complete protection with L-gamma-glutamyl-L-2-aminobutanoate, L-Glu + ATP, and ADP
S-sulfohomocysteine
-
-
S-sulfohomocysteine
-
D-enantiomer and L-enantiomer, ATP is not required for inactivation, noncovalent binding of close to 1 mol of inactivator per mol of enzyme, mixed-type inhibition
additional information
inhibition mechanisms, no inhibition by L-homocysteine sulfonate
-
additional information
inhibition mechanisms, no inhibition by L-homocysteine sulfonate
-
additional information
-
protein-supplemented diet inhibits expression of heavy subunit
-
additional information
-
7,12-dimethylbenz[a]anthracene does not affect GCS enzyme activity in gut tissue
-
additional information
7,12-dimethylbenz[a]anthracene does not affect GCS enzyme activity in gut tissue
-
additional information
-
oxidative stress dramatically affects GCL holoenzyme formation and activity
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Huang, C.S.; Moore, W.R.; Meister, A.
On the active site thiol of gamma-glutamylcysteine synthetase: relationship to catalysis, inhibition, and regulation
Proc. Natl. Acad. Sci. USA
85
2464-2468
1988
Escherichia coli, Rattus norvegicus
brenda
Moore, W.; Wiener, H.L.; Meister, A.
Inactivation of gamma-glutamylcysteine synthetase, but not of glutamine synthetase, by S-sulfocysteine and S-sulfohomocysteine
J. Biol. Chem.
262
16771-16777
1987
Rattus norvegicus
brenda
Seelig, G.F.; Meister.A.
gamma-Glutamylcysteine synthetase from erythrocytes
Methods Enzymol.
113
390-392
1985
Rattus norvegicus
brenda
Seelig, G.F.; Meister, A.
Glutathione biosynthesis: gamma-Glutamylcysteine synthetase from rat kidney
Methods Enzymol.
113
379-390
1985
Rattus norvegicus
brenda
Seelig, G.F.; Simondsen, R.P.; Meister, A.
Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits
J. Biol. Chem.
259
9345-9347
1984
Rattus norvegicus
brenda
Seelig, G.F.; Meister, A.
gamma-Glutamylcysteine synthetase from erythrocytes
Anal. Biochem.
141
510-514
1984
Rattus norvegicus
brenda
Seelig, G.F.; Meister, A.
gamma-Glutamylcysteine synthetase. Interaction of an essential sulfhydryl group
J. Biol. Chem.
259
3534-3538
1984
Rattus norvegicus
brenda
Griffith, O.W.; Meister, A.
Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
J. Biol. Chem.
254
7558-7560
1979
Rattus norvegicus
brenda
Griffith, O.W.; Anderson, M.E.; Meister, A.
Inhibition of glutathione biosynthesis by prothionine sulfoximine (S-n-propyl homocysteine sulfoximine), a selective inhibitor of gamma-glutamylcysteine synthetase
J. Biol. Chem.
254
1205-1210
1979
Rattus norvegicus
brenda
Sekura, R.; Meister, A.
gamma-Glutamylcysteine synthetase. Further purification, half of the sites" reactivity, subunits, and specificity
J. Biol. Chem.
252
2599-2605
1977
Rattus norvegicus
brenda
Orlowski, M.; Meister, A.
gamma-Glutamylcysteine synthetase (rat kidney)
Methods Enzymol.
17B
495-500
1971
Rattus norvegicus
-
brenda
Richman, P.G.; Orlowski, M.; Meister, A.
Inhibition of gamma-glutamylcysteine synthetase by L-methionine-S-sulfoximine
J. Biol. Chem.
248
6684-6690
1973
Rattus norvegicus
brenda
Davis, J.S.; Balinsky, J.B.; Harington, J.S.; Shepherd, J.B.
Assay, purification, properties and mechanism of action of gamma-glutamylcysteine synthetase from the liver of the rat and Xenopus laevis
Biochem. J.
133
667-678
1973
Rattus norvegicus, Xenopus laevis
brenda
Yip, B.; Rudolph, F.B.
The kinetic mechanism of rat kidney gamma-glutamylcysteine synthetase
J. Biol. Chem.
251
3563-3568
1976
Rattus norvegicus
brenda
Simondsen, R.P.; Meister, A.
Interaction of the D-isomer of gamma-methylene glutamate with an active site thiol of gamma-glutamylcysteine synthetase
J. Biol. Chem.
261
17134-17137
1986
Rattus norvegicus
brenda
Chang, L.
The functional involvement of Lys-38 in the heavy subunit of rat kidney gamma-glutamylcysteine synthetase: chemical modification and mutagenesis studies
J. Protein Chem.
15
321-326
1996
Rattus norvegicus
brenda
Chang, L.; Chang, C.
Biochemical regulation of the activity of gamma-glutamylcysteine synthetase from rat liver and kidney by glutathione
Biochem. Mol. Biol. Int.
32
697-703
1994
Rattus norvegicus
brenda
Huang, C.S.; Anderson, M.E.; Meister, A.
Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase
J. Biol. Chem.
268
20578-20583
1993
Rattus norvegicus
brenda
Huang, C.S.; Chang, L.S.; Anderson, M.E.; Meister, A.
Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase
J. Biol. Chem.
268
19675-19680
1993
Rattus norvegicus
brenda
Griffith, O.W.; Mulcahy, R.T.
The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase
Adv. Enzymol. Relat. Areas Mol. Biol.
73
209-267
1999
Ascaris suum, Bos taurus, [Candida] boidinii, Ovis aries, Nicotiana tabacum, no activity in Entamoeba histolytica, Proteus mirabilis, Sus scrofa, Xenopus sp., no activity in Giardia sp., Mus musculus (A0A0H2UNM8), Mus musculus (P97494), Escherichia coli (P0A6W9), Rattus norvegicus (P19468), Rattus norvegicus (P48508), Saccharomyces cerevisiae (P32477), Arabidopsis thaliana (P46309), Homo sapiens (P48506), Homo sapiens (P48507), Homo sapiens, Leishmania tarentolae (P90557), Schizosaccharomyces pombe (Q09768), Trypanosoma brucei (Q26820), Acidithiobacillus ferrooxidans (Q56277)
brenda
Gegg, M.E.; Clark, J.B.; Heales, S.J.R.
Determination of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection
Anal. Biochem.
304
26-32
2002
Rattus norvegicus
brenda
Huber, W.W.; Scharf, G.; Rossmanith, W.; Prustomersky, S.; Grasl-Kraupp, B.; Peter, B.; Turesky, R.J.; Schulte-Hermann, R.
The coffee components kahweol and cafestol induce g-glutamylcysteine synthetase, the rate limiting enzyme of chemoprotective glutathione synthesis, in several organs of the rat
Arch. Toxicol.
75
685-694
2002
Rattus norvegicus
brenda
Huang, Z.A.; Yang, H.; Chen, C.; Zeng, Z.; Lu, S.C.
Inducers of gamma-glutamylcysteine synthetase and their effects on glutathione synthetase expression
Biochim. Biophys. Acta
1493
48-55
2000
Rattus norvegicus
brenda
Wild, A.C.; Mulcahy, R.T.
Regulation of gamma-glutamylcysteine synthetase subunit gene expression: insights into transcriptional control of antioxidant defenses
Free Radic. Res.
32
281-301
2000
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Yang, H.; Zeng, Y.; Lee, T.D.; Yang, Y.; Ou, X.; Chen, L.; Haque, M.; Rippe, R.; Lu, S.C.
Role of AP-1 in the coordinate induction of rat glutamate-cysteine ligase and glutathione synthetase by tert-butylhydroquinone
J. Biol. Chem.
277
35232-35239
2002
Rattus norvegicus
brenda
Shukla, G.S.; Chiu, J.; Hart, B.A.
Enhanced expression of pulmonary gamma-glutamylcysteine synthetase heavy subunit in rats exposed to cadmium aerosols
Toxicol. Appl. Pharmacol.
163
249-259
2000
Rattus norvegicus
brenda
Tsai-Turton, M.; Luderer, U.
Gonadotropin regulation of glutamate cysteine ligase catalytic and modifier subunit expression in rat ovary is subunit and follicle stage specific
Am. J. Physiol.
289
E391-402
2005
Rattus norvegicus (P19468)
brenda
Lee, J.I.; Kang, J.; Stipanuk, M.H.
Differential regulation of glutamate-cysteine ligase subunit expression and increased holoenzyme formation in response to cysteine deprivation
Biochem. J.
393
181-190
2006
Rattus norvegicus
brenda
Chik, K.; Flourie, F.; Arab, K.; Steghens, J.P.
Kinetic measurement by LC/MS of gamma-glutamylcysteine ligase activity
J. Chromatogr. B
827
32-38
2005
Rattus norvegicus (P19468), Homo sapiens (P48506), Homo sapiens
brenda
Hansen, J.M.; Lee, E.; Harris, C.
Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and visceral yolk sac
Toxicol. Sci.
81
371-378
2004
Rattus norvegicus
brenda
Dasgupta, A.; Das, S.; Sarkar, P.K.
Thyroid hormone promotes glutathione synthesis in astrocytes by up regulation of glutamate cysteine ligase through differential stimulation of its catalytic and modulator subunit mRNAs
Free Radic. Biol. Med.
42
617-626
2007
Rattus norvegicus
brenda
Wu, H.; White, C.C.; Isanhart, J.P.; McBride, T.J.; Kavanagh, T.J.; Hooper, M.J.
Optimization and application of glutamate cysteine ligase measurement in wildlife species
Ecotoxicol. Environ. Saf.
72
572-578
2008
Anas platyrhynchos, Mus musculus, Rattus norvegicus
brenda
Pereda, J.; Escobar, J.; Sandoval, J.; Rodriguez, J.L.; Sabater, L.; Pallardo, F.V.; Torres, L.; Franco, L.; Vina, J.; Lopez-Rodas, G.; Sastre, J.
Glutamate cysteine ligase up-regulation fails in necrotizing pancreatitis
Free Radic. Biol. Med.
44
1599-1609
2008
Rattus norvegicus
brenda
Franklin, C.C.; Backos, D.S.; Mohar, I.; White, C.C.; Forman, H.J.; Kavanagh, T.J.
Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligase
Mol. Aspects Med.
30
86-98
2008
Arabidopsis thaliana, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Kaufmann, Y.; Todorova, V.K.; Luo, S.; Klimberg, V.S.
Glutamine affects glutathione recycling enzymes in a DMBA-induced breast cancer model
Nutr. Cancer
60
518-525
2008
Rattus norvegicus, Rattus norvegicus (P19468)
brenda
Petrovic, V.; Buzadzic, B.; Korac, A.; Vasilijevic, A.; Jankovic, A.; Korac, B.
L-Arginine supplementation induces glutathione synthesis in interscapular brown adipose tissue through activation of glutamate-cysteine ligase expression: The role of nitric oxide
Chem. Biol. Interact.
182
204-212
2009
Rattus norvegicus
brenda
Chen, C.N.; Brown-Borg, H.M.; Rakoczy, S.G.; Ferrington, D.A.; Thompson, L.V.
Aging impairs the expression of the catalytic subunit of glutamate cysteine ligase in soleus muscle under stress
J. Gerontol. A Biol. Sci. Med. Sci.
65
129-137
2010
Rattus norvegicus
brenda
Hosomi, H.; Akai, S.; Minami, K.; Yoshikawa, Y.; Fukami, T.; Nakajima, M.; Yokoi, T.
An in vitro drug-induced hepatotoxicity screening system using CYP3A4-expressing and gamma-glutamylcysteine synthetase knockdown cells
Toxicol. In Vitro
24
1032-1038
2010
Rattus norvegicus (P19468)
brenda
Morita, M.; Akai, S.; Hosomi, H.; Tsuneyama, K.; Nakajima, M.; Yokoi, T.
Drug-induced hepatotoxicity test using gamma-glutamylcysteine synthetase knockdown rat
Toxicol. Lett.
189
159-165
2009
Rattus norvegicus
brenda
Park, S.H.; Jang, J.H.; Chen, C.Y.; Na, H.K.; Surh, Y.J.
A formulated red ginseng extract rescues PC12 cells from PCB-induced oxidative cell death through Nrf2-mediated upregulation of heme oxygenase-1 and glutamate cysteine ligase
Toxicology
278
131-139
2010
Rattus norvegicus
brenda
Huang, J.Y.; Chuang, J.I.
Fibroblast growth factor 9 upregulates heme oxygenase-1 and gamma-glutamylcysteine synthetase expression to protect neurons from 1-methyl-4-phenylpyridinium toxicity
Free Radic. Biol. Med.
49
1099-1108
2010
Rattus norvegicus
brenda
Sikalidis, A.K.; Mazor, K.M.; Lee, J.I.; Roman, H.B.; Hirschberger, L.L.; Stipanuk, M.H.
Upregulation of capacity for glutathione synthesis in response to amino acid deprivation: regulation of glutamate-cysteine ligase subunits
Amino Acids
46
1285-1296
2014
Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Ferguson, G.; Bridge, W.
Glutamate cysteine ligase and the age-related decline in cellular glutathione the therapeutic potential of gamma-glutamylcysteine
Arch. Biochem. Biophys.
593
12-23
2016
Rattus norvegicus (P19468 AND P48508)
brenda