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ATP + alpha-ethyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-ethyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + alpha-methyl-L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate
ATP + alpha-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
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-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 + 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
ATP + D-Glu + L-Cys
ADP + phosphate + D-Glu-L-Cys
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
ADP + phosphate + 5-oxoproline
-
-
ir
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-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
ATP + L-Glu + beta-cyano-L-alanine
ADP + phosphate + gamma-L-Glu-beta-cyano-L-alanine
-
-
ir
ATP + L-Glu + butylamine
ADP + phosphate + N-butyl-L-glutamine
-
-
-
-
?
ATP + L-Glu + D-Cys
ADP + phosphate + gamma-L-Glu-D-Cys
ATP + L-Glu + DL-allylglycine
ADP + phosphate + gamma-L-Glu-DL-allylglycine
ATP + L-Glu + DL-beta-amino-iso-butyrate
ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
-
ir
ATP + L-Glu + ethylamine
ADP + phosphate + N-ethyl-L-glutamine
-
-
-
-
?
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 + Gly
ADP + phosphate + gamma-L-Glu-Gly
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-2-aminobutyrate
ADP + phosphate + gamma-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
ATP + L-Glu + L-alanine
ADP + phosphate + gamma-L-Glu-L-alanine
ATP + L-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-L-Glu-L-alpha-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-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
ATP + L-Glu + L-homocysteine
ADP + phosphate + gamma-L-Glu-L-homocysteine
ATP + L-Glu + L-homoserine
ADP + phosphate + gamma-L-Glu-L-homoserine
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-norleucine
ADP + phosphate + gamma-L-Glu-L-norleucine
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
ATP + L-Glu + L-serine
ADP + phosphate + gamma-L-Glu-L-serine
ATP + L-Glu + L-Thr
ADP + phosphate + gamma-L-Glu-L-Thr
-
-
-
-
?
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
ATP + L-Glu + L-valine
ADP + phosphate + gamma-L-Glu-L-valine
-
-
ir
ATP + L-Glu + methylamine
ADP + phosphate + N-methyl-L-glutamine
-
-
-
-
?
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-Cys
ADP + phosphate + gamma-L-Glu-S-methyl-L-Cys
ATP + L-Glu + S-methyl-L-cysteine
ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
-
ir
ATP + L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-(2-aminobutyrate)
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-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
-
-
?
additional information
?
-
ATP + alpha-methyl-L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate
-
-
-
-
?
ATP + alpha-methyl-L-glutamate + 2-aminobutyrate
ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate
-
-
-
-
?
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 + 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
-
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 + D-Cys
ADP + phosphate + gamma-L-Glu-D-Cys
-
-
-
-
?
ATP + L-Glu + D-Cys
ADP + phosphate + gamma-L-Glu-D-Cys
-
-
-
-
?
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
-
-
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
-
-
-
-
?
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-Ala
ADP + phosphate + gamma-L-Glu-L-Ala
-
-
-
-
?
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
?
-
rate-limiting step in glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
?
-
key regulatory enzyme in glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
?
-
-
-
-
?
ATP + L-Glu + L-Cys
?
-
glutathione biosynthesis
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
Bacterium cadaveris
-
-
-
-
?
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
-
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
-
-
-
-
?
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
-
-
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
-
-
-
-
?
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
-
-
?
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
-
-
-
-
?
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 the GSH biosynthesis
-
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
first and rate-limiting step in glutathione 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
-
-
-
-
?
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
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
-
?
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
-
-
-
-
?
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
Pseudomonas schuylkilliensis
-
-
-
-
?
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
-
-
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
r
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
-
-
-
-
?
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-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
-
-
-
-
?
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
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
-
-
-
-
?
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
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Streptococcus agalactiae serogroup 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 in form of MnATP2-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
ATP in form of MgATP2-
-
-
?
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
?
-
-
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
-
?
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
?
-
-
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
?
-
substrate specificity
-
?
additional information
?
-
substrate specificity
-
?
additional information
?
-
-
substrate specificity
-
?
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
?
-
-
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
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
-
rate-limiting enzyme in GSH biosynthesis
-
-
?
additional information
?
-
-
rate-limiting enzyme in GSH biosynthesis
-
-
?
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
?
-
-
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 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 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.
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-Glu + L-Cys
?
-
rate-limiting step in glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
?
-
key regulatory enzyme in glutathione biosynthesis
-
-
?
ATP + L-Glu + L-Cys
?
-
-
-
-
?
ATP + L-Glu + L-Cys
?
-
glutathione biosynthesis
-
-
?
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
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
-
the enzyme has key influence on glutathione homeostasis
-
?
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
-
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 GSH biosynthesis
-
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
-
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
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
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
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
-
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
-
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
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
-
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 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-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
-
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
-
ir
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
-
redox regulation of the enzyme, 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
-
-
-
?
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
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
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
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
-
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
-
-
-
-
?
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 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
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
-
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
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
-
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
-
-
-
?
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
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
Streptococcus agalactiae serogroup 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
first step in the biosynthesis of glutathione, pathway overview
-
-
?
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
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
-
-
-
-
?
additional information
?
-
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
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
?
-
-
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
?
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
additional information
?
-
-
rate-limiting enzyme in GSH biosynthesis
-
-
?
additional information
?
-
-
rate-limiting enzyme in GSH biosynthesis
-
-
?
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
?
-
-
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
-
?
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
?
-
-
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 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 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
?
-
most of the GSH produced in this pathway is converted to trypanothione
-
?
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(2S)-2-amino-4-[(2R,S)-2-carboxy-3-hydroxypropyl-(R,S)-sulfonimidoyl]butanoic acid
-
slow-binding, irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
(2S)-2-amino-4-[(2R,S)-2-carboxy-3-phenylpropyl-(R,S)-sulfonimidoyl]butanoic acid
-
weak, reversible inhibition
(2S)-2-amino-4-[(2R,S)-2-carboxybutyl-(R,S)-sulfonimidoyl]butanoic acid
-
slow-binding, irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
(2S)-2-amino-4-[(2R,S)-2-carboxyhexyl-(R,S)-sulfonimidoyl]butanoic acid
-
slow-binding, irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
(2S)-2-amino-4-[(2R,S)-2-carboxyoctyl-(R,S)-sulfonimidoyl]butanoic acid
-
weak, reversible inhibition
(2S)-2-amino-4-[(2R,S)-2-carboxypropyl-(R,S)-sulfonimidoyl]butanoic acid
-
slow-binding, irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
(2S)-2-amino-4-[2-carboxyethyl-(R,S)-sulfonimidoyl]butanoic acid
-
slow-binding, irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
4-hydroxy-2-nonenal
-
treatment with 4-hydroxy-2-nonenal results in the dose-dependent adduction of both monomeric GCLC and GCLM. 4-Hydroxy-2-nonenal-mediated adduction of monomeric GCLC results in a dose-dependent increase in GCLC enzymatic activity. Treatment of GCL holoenzyme causes a dose-dependent decrease in GCL activity. 4-Hydroxy-2-nonenal-mediated inhibition of GCL holoenzyme activity is associated with a reduction in the levels of heterodimeric GCL holoenzyme complex due to increase in high molecular weight complexes. 4-Hydroxy-2-nonenal modification simultaneously activates monomeric GCLC activity and prevents its ability to heterodimerize with GCLM and form functional GCL holoenzyme
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
acetaminophen
-
treatment promotes the loss of glutamate cysteine ligase in liver. Activation of glycogen synthase kinase 3beta is a key mediator of the initial phase of acetaminophen-induced liver injury through modulating GCL and Mcl-1 degradation, as well as JNK activation in liver. The silencing of glycogen synthase kinase 3beta decreases the loss of hepatic GCL, and promotes greater GSH recovery in liver following acetaminophen treatment
Ag+
-
complete inactivation
alpha-Methyl-DL-glutamate
-
-
antimony
-
heterozygous mutants with one allele inactivated show a significant decreased survival in the presence of antimony
ATP
-
substrate inhibition of mutant R179A, when only one other substrate is saturating
carbon tetrachloride
-
a single dose of 1589 mg/kg body weight of carbon tetrachloride causes changes in CGL activity and glutathione content in multiple organs of deer mice. Hepatic GCL activity and GSH content are depleted substantially, renal GCL activity increases. Blood, brain and heart GCL activities increase, whereas GSH contents decrease significantly
ciprofibrate
-
inhibits expression of heavy subunit
cis-1-Amino-1,3-dicarboxycyclohexane
-
-
Co2+
-
22% residual activity
Cu2+
-
27% residual activity
D-3-amino-1-chloro-2-pentanone
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
gamma-glutamylcysteine
-
-
gamma-methylene-D-glutamate
-
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-alpha-aminobutyrate
-
substrate inhibition of mutant R179A, when only one other substrate is saturating
L-buthionine sulfone
competitive, reversible
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-R,S-sulfoximine
i.e. BSO, specific, irreversible
L-buthionine-R-sulfoximine
L-buthionine-S-sulfoximine
L-buthionine-SR-sulfoximine
L-glutamic acid gamma-monohydroxamate
-
ATP-dependent irreversible inactivation, loss of 90% activity within 3 days, inactivation mechanism, no inactivation occurs in absence of ATP or with AMP-PNP
L-glutamine
inhibition of enzyme activity in tumor tissue
L-Homocysteine sulfinate
-
-
L-methionine
-
inhibits expression of heavy subunit
lipopolysaccharides
-
inhibits expression of heavy subunit
-
methionine
-
inhibits induction of GSH1 expression, independently of GSH
N-[2(2-Aminoethyl)-dithioethyl]4-azido-2-nitrobenzeneamine
-
-
NF-kappaB
-
inhibits induction of enzyme expression by other substances, e.g. buthionine sulfoximine or tert-butylhydroquinone
-
Ni2+
-
complete inactivation
oxidative stress
-
heterozygous mutants with one allele inactivated are more susceptible to oxidative stresses in vitro as promastigotes and show decreased survival inside activated macrophages producing reactive oxygen or nitrogen species
-
Pb2+
-
in deer mice exposed to Pb, or Pb together with Cu and Zn via drinking water for 4 weeks. GCL activities are not significantly affected by treatments. Metal-contaminated soils do not lead to significant effects in pups via lactation, 50-day exposure alters glutathione content marginally, while 100-day exposure results in marked GCL activity depletion. After 100-day exposure, GCL activities of the medium soil-, high soil- and Pb-treated deer mice are only 53%, 40% and 46% of the control, respectively
S-(S-Methyl)cysteamine
-
-
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+
Thiocholine disulfide
-
-
threo-beta-Hydroxy-DL-glutamate
-
-
threo-gamma-Hydroxy-L-glutamate
-
-
trans-1-Amino-1,3-dicarboxycyclohexane
-
-
Trinitrobenzene sulfonate
4-Methylene glutamate
-
no inhibition
4-Methylene glutamate
-
-
buthionine sulfoximine
-
specific inhibitor of GCL
buthionine sulfoximine
-
-
buthionine sulfoximine
-
-
buthionine sulfoximine
-
-
buthionine sulfoximine
-
only in presence of ATP
buthionine sulfoximine
-
complete inhibition
buthionine sulfoximine
-
GCL mediates the phosphorylation of buthionine sulfoximine, which is required for its tight and irreversible binding to the active site of GCL
buthionine sulfoximine
-
GCL mediates the phosphorylation of buthionine sulfoximine, which is required for its tight and irreversible binding to the active site of GCL
buthionine sulfoximine
an irreversible GCL inhibitor, abolishes the beta-carotene-induced GSH increase without affecting the beta-carotene-induced GCL protein expression
buthionine sulfoximine
-
-
buthionine sulfoximine
specific inhibitor of GCL
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
buthionine sulfoximine
-
specific inhibitor of GCL
buthionine sulfoximine
-
-
Cd2+
-
0.2 mM, activity is reduced by 35%
Cd2+
-
no residual activity
cystamine
-
cystamine
-
no inhibition
cystamine
-
completely reversible by DTT
cystamine
-
7.5 mM MgCl2 + 7.5 mM L-Glu protect
cystamine
-
L-Glu protects, ATP enhances rate of inactivation
cystamine
-
irreversible inactivation of the wild-type enzyme, loss of 75% activity within 10 min at 0.01 mM, binds to active site Cys319 and in this way blocks the binding of substrate to the enzyme, no inhibition of the mutant C319A enzyme
cysteamine
-
rapid inactivation, reversible by thiols
cysteamine
rapid inactivation, reversible by thiols
cysteamine
-
inactivation of wild-type enzyme and mutant C553G after 90 min at 4°C, 0.2 mM cysteamine and 2 mM ATP
cysteamine
-
complete inhibition
cysteamine
rapid inactivation, reversible by thiols
cysteamine
-
rapid inactivation, reversible by thiols
cysteamine
rapid inactivation, reversible by thiols
cysteamine
-
rapid inactivation, reversible by thiols
cysteamine
-
wild-type enzyme is inhibited by 75% at 0.01 mM after 10 min, complete irreversible inhibition at 10 mM, the mutant C319Ais completely resistant to cysteamine
D-3-amino-1-chloro-2-pentanone
-
highly potent irreversible inactivator
D-3-amino-1-chloro-2-pentanone
-
dithiothreitol
-
-
dithiothreitol
-
inhibition of wild-type holoenzyme and C553G mutant holoenzyme, the latter is more sensitive
DTT
-
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
-
feedback inhibition
glutathione
feedback inhibition, non-competitive inhibitor versus both glutamate and cysteine
glutathione
-
feed-back inhibition
glutathione
feedback inhibition
glutathione
-
feed-back inhibition
glutathione
-
feed-back inhibition; GSH inhibits, GSSG has no inhibitory effect
glutathione
-
feedback inhibition, subunit GCLM increases the Ki for GSH-mediated feedback inhibition of GCL, competitive to glutamate
glutathione
-
the cataytic subunit GCLC is feddback inhibited by GSH
glutathione
-
feedback inhibition, subunit GCLM increases the Ki for GSH-mediated feedback inhibition of GCL, competitive to glutamate
glutathione
compared with the holoenzyme, the catalytic GCLc monomer shows lower enzymatic activity but higher sensitivity to feedback inhibition by GSH
glutathione
feedback inhibition
glutathione
-
feedback inhibition
glutathione
-
competitive to L-Glu, non-competitive to ATP and L-Cys
glutathione
reduced glutathione (GSH) acts as a probably allosteric inhibitor of rPhGshA II. The oxidised form of glutathione (GSSG) inhibits the enzyme with a more complex inhibition profile, due to the complete monoglutathionylation of rPhGshA II on Cys 386, as proved by mass spectrometry data. Inhibition profiles and kinetics of GSH and GSSG, overview
glutathione
-
feed-back inhibition
glutathione
-
whole enzyme and large subunit inhibited
glutathione
-
inhibited by both GSSG and GSH
glutathione
-
feedback inhibition, subunit GCLM increases the Ki for GSH-mediated feedback inhibition of GCL, competitive to glutamate
glutathione
feedback-regulation. The structure of the GCL-glutathione complex to 2.5 A resolution indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+-coordination in the ATP-binding site
glutathione
the L-glutamate L-cysteine ligase of enzyme gshF is feedback inhibited by GSH
glutathione
substrate inhibition
glutathione
-
feedback inhibition
glutathione
-
GSSG inhibits, GSH has no inhibitory effect
GSH
feedback inhibition, the gamma-GCS activity is inhibited by a high concentration of GSH
GSH
feedback inhibition, the gamma-GCS activity is inhibited by a high concentration of GSH
GSH
-
feedback inhibition
GSH
-
feedback inhibition
GSH
-
feedback inhibition, the elimination of disulfide bridges between the subunits renders the enzyme more sensitive to inhibition
GSH
-
reduced, feedback inhibition of wild-type and mutants
GSH
-
noncompetitive to L-glutamate, inhibition is not dependent on reduction of disulfide bonds between the 2 subunits in the holoenzyme
GSH
-
feedback inhibition, mutant R127C is not sensitive
GSH
-
feedback inhibition, acts on the heavy catalytic subunit
GSH
-
competitive feedback inhibition with respect to L-glutamate
GSH
-
feedback inhibition, acts on the heavy catalytic subunit
GSH
-
noncompetitive versus L-glutamate or ATP
GSH
-
feedback inhibition
GSH
-
feedback inhibition
GSH
feedback inhibition, competitive to L-Glu
GSH
-
feedback inhibition, acts on the heavy catalytic subunit
GSH
-
feedback inhibition
GSH
-
regulatory function, represses expression of GSH1 gene
GSH
-
wild-type enzyme is nearly uninhibited by GSH (Ki about 140 mM), shorter gamma-glutamylcysteine synthetase domain constructs are strongly inhibited (Ki about 15 mM)
GSH
-
feedback inhibition
GSH
-
feedback inhibition
Hg2+
-
-
Hg2+
-
no residual activity
iodoacetamide
-
-
K+
-
-
L-buthionine sulfoximine
-
95% inhibition at 0.001 mM
L-buthionine sulfoximine
-
-
L-buthionine-R-sulfoximine
-
L-buthionine-R-sulfoximine
-
L-buthionine-R-sulfoximine
mechanism-based, competitive, reversible
L-buthionine-S-sulfoximine
strong inhibition
L-buthionine-S-sulfoximine
mechanism-based inhibitor, in contrary to the mammalian enzyme form, the Escherichia coli enzyme is inhibited more weakly and slowly in presence of Mg2+, replacement of the metal by Mn2+ leads to increased binding affinity and inactivation rate
L-buthionine-S-sulfoximine
strong inhibition
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
L-buthionine-S-sulfoximine
-
specific inhibitor
L-buthionine-S-sulfoximine
mechanism-based inhibitor. The crystal structure of the enzyme complex to 2.2 A resolution confirms that L-buthionine-S-sulfoximine is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization
L-buthionine-S-sulfoximine
-
competitive with L-glutamate
L-buthionine-S-sulfoximine
-
irrversible inactivation, no inhibition of mutant R366A
L-buthionine-SR-sulfoximine
-
irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
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. After subacute exposure, low doses increases GCL activity and GSH content in liver by 48.3% and 54.4%, respectively. High doses reduce GCL activities significantly in liver and kidney to 31.2% and 43.0% of the control, respectively
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-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
methionine sulfoximine
-
methionine sulfoximine
-
-
methionine sulfoximine
-
-
methionine sulfoximine
-
-
methionine sulfoximine
-
and analogs, no effect on glutamine synthetase
methionine sulfoximine
-
-
methionine sulfoximine
-
of the 4 stereoisomers only L-methionine-S-sulfoximine inhibits
methionine sulfoximine
competitive and reversible
MgATP2-
although the enzyme preparation shows a strict requirement for MgATP2- for gamma-glutamylcysteine synthesis, preincubation of the homogenate under phosphorylating conditions with MgATP2- also causes a maximal inhibition of 89%
MgATP2-
although the enzyme preparation shows a strict requirement for MgATP2- for gamma-glutamylcysteine synthesis, preincubation of the homogenates under phosphorylating conditions with MgATP2- also causes a maximal inhibition of 94%, 77%, 85%, 87%, 83% and 95% in cerebellum, hippocampus, brainstem, striatum, cortex and heart
Na+
-
72.7% inhibition at 300 mM
Na+
69.2% inhibition at 300 mM
Na+
-
79.6% inhibition at 300 mM
NAD+
-
-
NADH
-
-
NADP+
-
-
NADPH
-
-
NEM
-
-
PCMB
-
-
Prothionine sulfoximine
-
-
Prothionine sulfoximine
-
i.e. S-n-propyl homocysteine sulfoximine; no effect on glutamine synthetase
S-butyl-DL-homocysteine-SR-sulfoximine
-
S-butyl-DL-homocysteine-SR-sulfoximine
-
S-sulfocysteine
-
no inhibition
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
-
no inhibition
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
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+
Trinitrobenzene sulfonate
inactivates the enzyme
Zn2+
-
0.2 mM, activity is reduced by 19%
Zn2+
-
21% residual activity
additional information
-
no inhibition by DTT
-
additional information
no inhibition by buthionine sulfoximine
-
additional information
-
no inhibition by buthionine sulfoximine
-
additional information
no inhibition by cysteamine or slowly at high concentration
-
additional information
-
no inacivationwith ATP alone or with L-aspartic acid gamma-monohydroxamate
-
additional information
-
the inhibition mode and potency of the different sulfoximines is highly dependent on the stereochemistry at the sulfoximine sulfur atom, overview
-
additional information
no inhibition by L-buthionine-R-sulfoximine
-
additional information
-
no inhibition by L-buthionine-R-sulfoximine
-
additional information
-
the genotype of GLCLC is associated with drug sensitivity or resistance, respectively, sensitivity of different genotypes to diverse drugs, overview
-
additional information
-
oxidative stress dramatically affects GCL holoenzyme formation and activity
-
additional information
-
decrease of enzyme activity in hypoxia: 20% after 6 h, 17% after 12 h, 23% after 24 h, hypoxia-induced decrease in enzyme activity may be prevented by MAPK inhibition and catalase
-
additional information
no inhibition by alpha-ethyl-methionine sulfoximine
-
additional information
no inhibition by alpha-ethyl-methionine sulfoximine
-
additional information
-
oxidative stress dramatically affects GCL holoenzyme formation and activity
-
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
-
oxidative stress dramatically affects GCL holoenzyme formation and activity
-
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
-
no significant inhibition by cystamine, L-methionine-SR-sulfoximine and GSH
-
additional information
insensitive to feedback inhibition caused by GSH even at 20 mM
-
additional information
-
no inhibition by DTT
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(4-amino-2-methyl-5-pyridimidyl)-methyl-3-(2-chloroethyl)-3-nitrosurea
-
induces expression of heavy subunit
2,3-dimethoxy-1,4-naphthoquinone
2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)-acetamide
-
i.e. metolachlor, a herbicide that decreases the plant growth and and biomass, induction of enzyme expression, enhanced enzyme activity leads to enhanced detoxification activity
2-chloro-N-(ethoxymethyl)-N-(2-ethyl-6-methylphenyl)-acetamide
-
i.e. acetochlor, a herbicide that decreases the plant growth and and biomass, induction of enzyme expression, enhanced enzyme activity leads to enhanced detoxification activity
6-Hydroxydopamine
-
induces expression of heavy subunit
activator protein 1
-
i.e. AP-1, is required for basal expression of the enzyme
-
adriamycin
-
induces expression of heavy subunit
apigenin
-
nearly 2fold induction of the heavy subunit gene promotor and heavy subunit expression
apocynin
-
induces expression of heavy subunit
beta-naphthoflavone
-
induces expression of heavy subunit
butylated hydroxyanisole
-
induces expression of heavy and light subunit
butylated hydroxytoluene
-
induces expression of heavy subunit
cadmium aerosols
-
2.4 mg Cd/m3, enhance in the lung the expression of the enzyme's heavy, catalytic subunit gamma-GCS-HS by 4.5fold after 15 min, 8fold after 6 h, increase in enzyme activity and GSH production rate
-
cafestol
-
coffee component, induction of the enzyme in vivo, especially in the liver up to 2.4fold, increase in expression of both enzyme subunits
caffeic acid
-
treatment of the cells with 100 and 500 microg/ml of caffeic acid increases gamma-GCS activities by 1.4- and 1.8fold compared to the control group, respectively. At the same doses of caffeic acid, the treated cells show increased levels of glutathione by 1.7- and 2.7fold compared to the control, respectively
carbon tetrachloride
-
a single dose of 1589 mg/kg body weight of carbon tetrachloride causes changes in CGL activity and glutathione content in multiple organs of deer mice. Hepatic GCL activity and GSH content are depleted substantially, renal GCL activity increases. Blood, brain and heart GCL activities increase, whereas GSH contents decrease significantly
cigarette smoke condensate
-
induces expression of heavy subunit
-
erythropoietin
-
induces expression of heavy subunit
-
Ethacrynic acid
-
induces expression of heavy subunit
ethanol
-
feeding in vivo increases the enzyme expression, treatment of hepatocytes induces the expression of only the heavy enzyme subunit
ethoxyquin
-
induces expression of heavy subunit
hydrocortisone
-
treatment of hepatocytes induces the expression of only the heavy enzyme subunit
Insulin
-
treatment of hepatocytes induces the expression of only the heavy enzyme subunit
-
interleukin-1 beta
-
induces expression of heavy subunit
-
iodoacetamide
-
induces expression of heavy subunit
kaempferol
-
2fold induction of the heavy subunit gene promotor and heavy subunit expression
kahweol
-
coffee component, induction of the enzyme in vivo, especially in the liver up to 2.4fold, increase in expression of both enzyme subunits
L-glutamine
enhanced enzyme activity in jejunal mucosa
mcCDC34
-
an ubiquitine conjugated protein, induces gamma-glutamylcysteine synthetase expression only in glutathione synthetase-dficient mutants, not in the wild-type
-
menadione
-
induces expression of heavy and light subunit
nitric oxide
-
induces expression of heavy and light subunit via direct exposure or interleukin-1 induced
oltipraz
-
induces expression of heavy subunit
onion extract
-
containing flavonoids, which increase the expression of both subunits of the enzyme in COS-1 cells
-
oxidative stress
-
activation of GCL occurrs within min of treatment and without any change in GCL protein levels, and coincides with an increase in the proportion of GCL catalytic subunit in the holoenzyme form. Likewise, GCL modifier subunit shifts from the monomeric form to holoenzyme and higher molecular weight species. Neither GCL activation, nor the formation of holoenzyme, requires a covalent intermolecular disulfide bridge between GCL catalytic subunit and GCL modifier subunit. In immunoprecipitation studies, a neutralizing epitope associated with enzymatic activity is protected following cellular oxidative stress. Thus, the N-terminal portion of GCL catalytic subunit may undergo a change that stabilizes the GCL holoenzyme. Results suggest a dynamic equilibrium between low- and high-activity forms of GCL, which is altered by transient oxidative stress
-
oxidized low density lipoprotein
-
induces expression of heavy subunit
-
phorone
-
induces expression of heavy subunit
Prostaglandin A2
-
induces expression of heavy subunit
pyrrolidine dithiocarbamate
quercetin
-
3fold induction of the heavy subunit gene promotor and heavy subunit expression, best at 0.05 mM, induction even of a distal part of the promotor sequence containing only 2 antioxidant-response/electrophile-response elements, i.e. ARE/EpRE
tert-butyl hydroquinone
-
induces expression of heavy and light subunit
Thioacetamide
-
induction of enzyme expression
2,3-dimethoxy-1,4-naphthoquinone
-
induces expression of heavy and light subunit
2,3-dimethoxy-1,4-naphthoquinone
-
induces expression of heavy and light subunit
4-hydroxy-2-nonenal
-
i.e. 4-HNE, inductor of enzyme expression, signals through the JNK pathway, most effective at 0.02 mM, time-dependence is different for GCLC and GCLM, overview, also activates the transcription factor complex AP-1 which itself activates expression of both enzyme subunits
4-hydroxy-2-nonenal
-
induces expression of heavy and light subunit
4-hydroxy-2-nonenal
-
4-hydroxy-2-nonenal causes a rapid dose- and time-dependent increase in A549 cell GCL activity. Maximal activation of GCL occurs at 30 min in response to 50 microM 4-hydroxy-2-nonenal
AP-1
-
transcription factor complex including Jun family members, drives expression of both enzyme subunit encoding genes, AP-1 complex is activated by 4-hydroxy-2-nonenal, enzyme induction can be blocked by membrane-permeable peptide-based JNK inhibitor JNKi, but not by inhibitors SB202190 or PD98059
-
AP-1
-
transcription factor induces enzyme expression
-
AP-1
-
transcription factor induces enzyme expression
-
AP-1
-
transcription factor induces enzyme expression
-
buthionine sulfoximine
-
induces expression of heavy and light subunit
buthionine sulfoximine
-
induction of enzyme expression
buthionine sulfoximine
-
induces expression of heavy and light subunit
diethyl maleate
-
induces expression of heavy and light subunit
diethyl maleate
-
induction of enzyme expression
Gly
-
stimulates
H2O2
-
40-50% increase in intracellular concentration induces enzyme expression 2fold to upregulate GSH production, GSH is required for detoxification, increase is reversible or preventable by peroxide-eliminating substances
H2O2
-
induces expression of heavy and light subunit
H2O2
induction of enzyme expression, increase in activity in V79 cells independent on transcription level
H2O2
induction of in enzyme expression and activity
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. After subacute exposure, low doses increases GCL activity and GSH content in liver by 48.3% and 54.4%, respectively. High doses reduce GCL activities significantly in liver and kidney to 31.2% and 43.0% of the control, respectively
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-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
methylmercuric hydroxide
-
induces expression of heavy subunit
methylmercuric hydroxide
-
induces expression of heavy subunit
pyrrolidine dithiocarbamate
-
time-, dose-, and Cu2+-dependent induction and increase in expression levels of the 2 subunits of the enzyme in HepG2 cells, mechanism, can be partially blocked by N-acetylcysteine and by copper chelator bathocuproine disulfonic acid
pyrrolidine dithiocarbamate
-
induces expression of heavy and light subunit
tert-butylhydroquinone
-
induces expression of heavy and light subunit
tert-butylhydroquinone
-
induction of enzyme expression
tert-butylhydroquinone
-
i.e. TBH, exerts a dose- and time-dependent increase in the mRNA level and promotor activity of the 2 genes encoding the enzyme subunits
additional information
In response to redox environment, AtGCL undergoes a reversible conformational change that modulates the enzymatic activity of the monomer
-
additional information
-
In response to redox environment, AtGCL undergoes a reversible conformational change that modulates the enzymatic activity of the monomer
-
additional information
both GCLC gene expression and total GSH levels increase 4 and 1.5fold, respectively, in response to hyperthermal stress, overview
-
additional information
-
both GCLC gene expression and total GSH levels increase 4 and 1.5fold, respectively, in response to hyperthermal stress, overview
-
additional information
-
multiple cis- and trans-elements have up-regulating effect on expression of the heavy catalytic subunit and of the regulatory light subunit, ionization radiation induces expression of heavy subunit, overview, effect of miscellaneous treatments on enzyme mRNA expression, overview
-
additional information
-
no increase in gene promotor activity by myricetin and sugar conjugates of quercetin, quercetin-3-glucoside and quercetin-3-rhamnoglucoside
-
additional information
-
no induction of enzyme production in HepG2 cells by overexpression of human cytochrome 3A4
-
additional information
-
extracts of Ginkgo biloba induces GCL catalytic subunit, GCLC, in HepG2 and Hep1c1c7 cell lines
-
additional information
-
resveratrol and 4-hydroxy-2-nonenal both increases GSH and the mRNA contents of both the catalytic GCLC and modulatory GCLM subunit of GCL, both agents show synergictic effects when applied together, overview. The cis-element Nrf2/EpRE signalling is involved in resveratrol-mediated induction of GCL genes
-
additional information
-
subunit GCLM increases the Vmax and Kcat of subunit GCLC, and decreases the Km for glutamate and ATP
-
additional information
-
the enzyme is induced by 4-hydroxy-2-nonenal through the c-Jun N-terminal kinase pathway, the regulation involves SHP-1, the protein-tyrosine phosphatase SH" domain containing phosphatase-1 in HBE1 cells, mechanism, overview
-
additional information
-
under low glucose levels insulin induces an approximate 2fold increase in expression of gamma-glutamylcysteine ligase catalytic subunit GCLc mRNA and protein, which does not lead to increased GSH levels in the cell
-
additional information
-
ionization radiation induces expression of heavy subunit, effect of miscellaneous treatments on enzyme mRNA expression, overview
-
additional information
-
induction of Gclc by homocysteine, ARE4 plays a direct role in mediating the induction, Nrf2 signalling is critical in homocysteine-induced activation of ARE4, overview
-
additional information
-
subunit GCLM increases the Vmax and Kcat of subunit GCLC, and decreases the Km for glutamate and ATP
-
additional information
GCL forms a homodimer under oxidizing conditions, and is activated more than threefold
-
additional information
-
GCL forms a homodimer under oxidizing conditions, and is activated more than threefold
-
additional information
high activity in 100-300 mM Tris buffer
-
additional information
-
effect of miscellaneous treatments on enzyme mRNA expression, overview
-
additional information
-
two-thirds partial hepatectomy increases the enzyme expression
-
additional information
-
GCLC expression is 3fold up-regulated 1 h after induction of edematous pancreatitis
-
additional information
-
subunit GCLM increases the Vmax and Kcat of subunit GCLC, and decreases the Km for glutamate and ATP
-
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7.3
(R)-beta-amino-iso-butyrate
-
-
13.3
(S)-beta-amino-iso-butyrate
-
-
2.9 - 10.4
2-aminobutyrate
1.3 - 150
4-aminobutyrate
0.86 - 1.3
gamma-L-Glu-L-Cys
0.14 - 10.4
L-2-aminobutanoate
0.8 - 5
L-2-aminobutyrate
5.4 - 6.1
L-2-aminobutyric acid
0.25 - 380
L-alpha-aminobutyrate
0.31
L-aminobutanoate
-
-
additional information
additional information
-
2.9
2-aminobutyrate
-
liver enzyme
10.4
2-aminobutyrate
-
L-Glu
1.3
4-aminobutyrate
-
pH 8.2, 37°C
20
4-aminobutyrate
-
mutant R366A, pH 8.0, 37°C
150
4-aminobutyrate
-
wild-type enzyme, pH 8.0, 37°C
0.0001
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
0.00014
ATP
-
pH 8.0, 25°C, wild-type enzyme
0.00019
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
0.00024
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
0.00025
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
0.00046
ATP
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
0.00053
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
0.022
ATP
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mn2+
0.06
ATP
-
pH 8.4, 37°C, mutant enzyme D520stop
0.065
ATP
-
pH 8.4, 37°C, mutant enzyme E494stop
0.065
ATP
-
pH 8.4, 37°C, mutant enzyme G441stop
0.066
ATP
-
pH 8.4, 37°C, mutant enzyme Y464stop
0.069
ATP
-
pH 8.4, 37°C, mutant enzyme K526A
0.071
ATP
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mg2+
0.071
ATP
-
wild-type, pH 8.0, 37°C
0.08
ATP
wild-type, pH 8.0
0.082
ATP
-
pH 8.4, 37°C, mutant enzyme R508stop
0.093
ATP
pH 8.0, 15°C, recombinant enzyme
0.1
ATP
-
mutant E489A, pH 8.0, 37°C, in presence of Mn2+
0.11
ATP
-
mutant R491A, pH 8.0, 37°C
0.14
ATP
-
mutant R179A, pH 8.0, 37°C
0.145
ATP
pH 7.5, 25°C, wild-type enzyme
0.199
ATP
pH 8.5, 40°C, recombinant His-tagged enzyme
0.26
ATP
-
mutant H370L, CGL holoenzyme, pH 8.0, 37°C
0.279
ATP
pH 7.5, 25°C, mutant H121Q
0.3
ATP
-
mutant P138L, CGL holoenzyme, pH 8.0, 37°C
0.31
ATP
pH 7.5, 25°C, mutant H121A
0.32
ATP
-
mutant E93A, pH 8.0, 37°C, in presence of Mg2+
0.352
ATP
pH 7.5, 25°C, mutant T117S
0.385
ATP
pH 8.5, 40°C, recombinant His-tagged enzyme
0.44
ATP
-
wild-type, CGL holoenzyme, pH 8.0, 37°C
0.445
ATP
pH 7.5, 25°C, mutant R167K
0.5
ATP
-
mutant R127C, CGL holoenzyme, pH 8.0, 37°C
0.622
ATP
-
pH 8.4, 37°C, mutant enzyme H144A
0.82
ATP
-
mutant P414L, catalytic subunit, pH 8.0, 37°C
0.87
ATP
-
37°C, pH 7.2, holoenzyme
0.969
ATP
pH 7.5, 25°C, mutant R248K
1.2
ATP
-
mutant Q321A, pH 8.0, 37°C, in presence of Mn2+
1.2
ATP
-
mutant R487A, pH 8.0, 37°C
1.3
ATP
-
mutant R474A, pH 8.0, 37°C
1.4
ATP
-
wild-type enzyme and mutant C319A, pH 8.0, 37°C
2
ATP
-
mutant E489A, pH 8.0, 37°C, in presence of Mg2+
2.68
ATP
-
wild-type, catalytic subunit, pH 8.0, 37°C
2.8
ATP
-
mutant R366A, pH 8.0, 37°C
3.57
ATP
-
mutant P138L, catalytic subunit, pH 8.0, 37°C
4.47
ATP
-
mutant R127C, catalytic subunit, pH 8.0, 37°C
5
ATP
-
37°C, pH 7.2, catalytic subunit GCLC
7
ATP
-
mutant T323A, pH 8.0, 37°C
25.3
ATP
-
pH 7, mutant enzyme C364S
31.6
ATP
-
pH 7, mutant enzyme C349S
37.5
ATP
-
pH 7, mutant enzyme C251S
40.3
ATP
-
pH 7, mutant enzyme C102S
42
ATP
-
pH 7, wild-type enzyme
45
ATP
-
above, mutant Q321A, pH 8.0, 37°C, in presence of Mg2+
0.3
cysteine
-
enzyme from embryo homogenate and from visceral yolk sac homogenate
2.7
cysteine
pH 7.0, 25°C, mutant DELTA85
0.86
gamma-L-Glu-L-Cys
-
catalytic subunit, pH 8.0, 37°C
1.3
gamma-L-Glu-L-Cys
-
holoenzyme, pH 8.0, 37°C
0.75
glutamate
-
enzyme from embryo homogenate
1.38
glutamate
-
enzyme from visceral yolk sac homogenate
9.1
glutamate
pH 7.0, 25°C, mutant DELTA85
0.14
L-2-aminobutanoate
-
-
0.8
L-2-aminobutanoate
-
recombinant heavy subunit
1
L-2-aminobutanoate
-
GTP
1.3
L-2-aminobutanoate
-
-
1.3
L-2-aminobutanoate
-
strain W
1.4
L-2-aminobutanoate
-
-
1.4
L-2-aminobutanoate
-
strain KM
1.4
L-2-aminobutanoate
-
L-Glu, holoenzyme
1.4
L-2-aminobutanoate
-
L-Glu, kidney enzyme
1.5
L-2-aminobutanoate
-
-
1.5
L-2-aminobutanoate
-
2-aminobutanoate, kidney enzyme
1.5
L-2-aminobutanoate
-
L-Glu, liver enzyme
10
L-2-aminobutanoate
-
-
10.4
L-2-aminobutanoate
-
-
0.8
L-2-aminobutyrate
37°C
1.4
L-2-aminobutyrate
37°C
1.7
L-2-aminobutyrate
-
recombinant catalytic subunit, pH 8.0, 37°C
3.4
L-2-aminobutyrate
-
recombinant holoenzyme, pH 8.0, 37°C
3.6
L-2-aminobutyrate
-
recombinant wild-type holoenzyme, pH 8.0, 37°C
5
L-2-aminobutyrate
-
recombinant mutant C553G holoenzyme, pH 8.0, 37°C
5.4
L-2-aminobutyric acid
-
wild-type enzyme, pH 8.0, 37°C
6.1
L-2-aminobutyric acid
-
mutant C319A, pH 8.0, 37°C
0.25
L-alpha-aminobutyrate
-
mutant R127C, pH 8.0, 37°C
0.31
L-alpha-aminobutyrate
-
-
1
L-alpha-aminobutyrate
-
1.3
L-alpha-aminobutyrate
-
2.3
L-alpha-aminobutyrate
-
2.39
L-alpha-aminobutyrate
-
wild-type enzyme, pH 8.0, 37°C
6
L-alpha-aminobutyrate
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mn2+
7.5
L-alpha-aminobutyrate
-
mutant T323A, pH 8.0, 37°C
9.4
L-alpha-aminobutyrate
-
mutant E489A, pH 8.0, 37°C, in presence of Mn2+
10
L-alpha-aminobutyrate
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mg2+
10
L-alpha-aminobutyrate
-
wild-type, pH 8.0, 37°C
14
L-alpha-aminobutyrate
-
mutant Q321A, pH 8.0, 37°C, in presence of Mn2+
15
L-alpha-aminobutyrate
-
mutant E489A, pH 8.0, 37°C, in presence of Mg2+
15
L-alpha-aminobutyrate
-
mutant R487A, pH 8.0, 37°C
18
L-alpha-aminobutyrate
-
mutant Q321A, pH 8.0, 37°C, in presence of Mg2+
34
L-alpha-aminobutyrate
-
mutant R366A, pH 8.0, 37°C
56
L-alpha-aminobutyrate
-
mutant R474A, pH 8.0, 37°C
380
L-alpha-aminobutyrate
-
mutant R179A, pH 8.0, 37°C
0.05
L-Cys
-
mutant R127C, catalytic subunit, pH 8.0, 37°C
0.07
L-Cys
-
wild-type, CGL holoenzyme, pH 8.0, 37°C
0.08
L-Cys
-
mutant P138L, catalytic subunit, pH 8.0, 37°C
0.1
L-Cys
-
wild-type, catalytic subunit, pH 8.0, 37°C
0.12
L-Cys
-
mutant R127C, CGL holoenzyme, pH 8.0, 37°C
0.138
L-Cys
-
pH 8.4, 37°C, mutant enzyme Y464stop
0.147
L-Cys
-
pH 8.4, 37°C, mutant enzyme K526A
0.16
L-Cys
-
mutant H370L, CGL holoenzyme, pH 8.0, 37°C
0.161
L-Cys
-
pH 8.4, 37°C, mutant enzyme D520stop
0.166
L-Cys
-
pH 8.4, 37°C, mutant enzyme G441stop
0.17
L-Cys
wild-type, pH 8.0
0.17
L-Cys
-
mutant P138L, CGL holoenzyme, pH 8.0, 37°C
0.17
L-Cys
-
mutant P414L, catalytic subunit, pH 8.0, 37°C
0.171
L-Cys
-
pH 8.4, 37°C, mutant enzyme E494stop
0.2
L-Cys
-
ATP, holoenzyme and recombinant heavy subunit
0.22
L-Cys
-
25°C, pH 8.2
0.26
L-Cys
-
pH 8.4, 37°C, mutant enzyme R508stop
1
L-Cys
-
pH 8.4, 37°C, mutant enzyme H144A
4 - 5.4
L-Cys
-
pH 7, mutant enzyme C364S
39.2
L-Cys
-
pH 7, mutant enzyme C251S
46.1
L-Cys
-
pH 7, mutant enzyme C349S
46.9
L-Cys
-
pH 7, wild-type enzyme
57.3
L-Cys
-
pH 7, mutant enzyme C102S
0.0001
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme
0.0001
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
0.00011
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
0.00011
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
0.00014
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
0.00014
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
0.00016
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
0.05
L-cysteine
pH 8.0, 15°C, recombinant enzyme
0.05
L-cysteine
pH 8.5, 40°C, recombinant His-tagged enzyme
0.059
L-cysteine
pH 7.5, 25°C, wild-type enzyme
0.1
L-cysteine
holoenzyme
0.1
L-cysteine
-
pH 8.2, 37°C
0.116
L-cysteine
pH 7.5, 25°C, mutant H121Q
0.13
L-cysteine
heavy subunit
0.14
L-cysteine
-
pH 8.4, 25°C
0.186
L-cysteine
pH 7.5, 25°C, mutant T117S
0.2
L-cysteine
heavy subunit and holoenzyme
0.22
L-cysteine
-
pH 8.2, 25°C
0.22
L-cysteine
-
37°C, pH 7.2, holoenzyme
0.27
L-cysteine
-
37°C, pH 7.2, catalytic subunit GCLC
0.5
L-cysteine
-
recombinant catalytic subunit, pH 8.0, 37°C
0.5
L-cysteine
-
recombinant mutant C553G holoenzyme, pH 8.0, 37°C
0.707
L-cysteine
pH 7.5, 25°C, mutant H121A
0.8
L-cysteine
-
recombinant holoenzyme, pH 8.0, 37°C
0.8
L-cysteine
-
recombinant wild-type holoenzyme, pH 8.0, 37°C
0.857
L-cysteine
pH 7.5, 25°C, mutant R248K
1.95
L-cysteine
pH 7.5, 25°C, mutant R167K
0.03
L-Glu
-
-
0.23
L-Glu
-
holoenzyme, pH 8.0, 37°C
0.44
L-Glu
-
mutant H370L, CGL holoenzyme, pH 8.0, 37°C
0.46
L-Glu
-
wild-type, CGL holoenzyme, pH 8.0, 37°C
0.63
L-Glu
-
mutant R127C, pH 8.0, 37°C
0.65
L-Glu
-
mutant P138L, CGL holoenzyme, pH 8.0, 37°C
0.68
L-Glu
-
mutant P138L, catalytic subunit, pH 8.0, 37°C
0.7
L-Glu
-
recombinant wild-type holoenzyme, pH 8.0, 37°C
0.77
L-Glu
-
mutant P414L, catalytic subunit, pH 8.0, 37°C
0.9
L-Glu
-
recombinant mutant C553G holoenzyme, pH 8.0, 37°C
1.14
L-Glu
-
wild-type, catalytic subunit, pH 8.0, 37°C
1.2
L-Glu
-
L-2-aminobutanoate
1.2
L-Glu
-
L-2-aminobutanoate
1.21
L-Glu
wild-type, pH 8.0
1.38
L-Glu
-
mutant R127C, catalytic subunit, pH 8.0, 37°C
1.38
L-Glu
-
mutant R127C, CGL holoenzyme, pH 8.0, 37°C
1.93
L-Glu
mutant C266A, pH 8.0
2 - 3
L-Glu
-
pH 8.4, 37°C, mutant enzyme Y464stop
2.15
L-Glu
mutant C266S, pH 8.0
2.2
L-Glu
-
catalytic subunit, pH 8.0, 37°C
2.6
L-Glu
-
wild-type enzyme, pH 8.0, 37°C
5.9
L-Glu
-
mutant C319A, pH 8.0, 37°C
7
L-Glu
-
pH 7, mutant enzyme C364S
7.16
L-Glu
-
wild-type enzyme, pH 8.0, 37°C
8.5
L-Glu
-
pH 7, mutant enzyme C102S
9.1
L-Glu
-
pH 7, wild-type enzyme
11.2
L-Glu
-
pH 7, mutant enzyme C349S
13.9
L-Glu
-
pH 7, mutant enzyme C251S
18.2
L-Glu
-
recombinant heavy subunit
22
L-Glu
-
pH 8.4, 37°C, mutant enzyme E494stop
24
L-Glu
-
pH 8.4, 37°C, mutant enzyme K526A
28.9
L-Glu
-
pH 8.4, 37°C, mutant enzyme D520stop
34.7
L-Glu
-
pH 8.4, 37°C, mutant enzyme R508stop
77
L-Glu
-
pH 8.4, 37°C, mutant enzyme G441stop
229
L-Glu
-
pH 8.4, 37°C, mutant enzyme H144A
0.0032
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
0.0039
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme
0.004
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
0.004
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
0.0041
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
0.0051
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
0.0053
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
0.24
L-glutamate
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mg2+
0.24
L-glutamate
-
wild-type, pH 8.0, 37°C
0.48
L-glutamate
-
37°C, pH 7.2, holoenzyme
0.5
L-glutamate
pH 7.5, 25°C, mutant R167K
0.61
L-glutamate
-
mutant R491A, pH 8.0, 37°C
0.7
L-glutamate
-
recombinant holoenzyme, pH 8.0, 37°C
0.82
L-glutamate
-
pH 8.4, 25°C
0.89
L-glutamate
-
mutant E489A, pH 8.0, 37°C, in presence of Mn2+
0.91
L-glutamate
-
25°C, recombinant His-tagged wild-type enzyme
0.92
L-glutamate
-
25°C, recombinant His-tagged wild-type catalytic subunit
0.953
L-glutamate
pH 7.5, 25°C, wild-type enzyme
0.97
L-glutamate
-
25°C, recombinant His-tagged wild-type catalytic subunit with recombinant His-tagged mutant modifier subunit C213S/C214S/C267S
1
L-glutamate
-
wild-type enzyme, pH 8.0, 37°C, in presence of Mn2+
1.1
L-glutamate
-
mutant E489A, pH 8.0, 37°C, in presence of Mg2+
1.1
L-glutamate
-
mutant Q321A, pH 8.0, 37°C, in presence of Mn2+
1.18
L-glutamate
pH 7.5, 25°C, mutant H121Q
1.2
L-glutamate
pH 8.0, 37°C
1.3
L-glutamate
-
mutant R487A, pH 8.0, 37°C
1.4
L-glutamate
holoenzyme
1.4
L-glutamate
-
holoenzyme
1.6
L-glutamate
-
mutant Q321A, pH 8.0, 37°C, in presence of Mg2+
1.6
L-glutamate
-
mutant R474A, pH 8.0, 37°C
1.6
L-glutamate
-
37°C, pH 7.2, catalytic subunit GCLC
1.7
L-glutamate
strain KM
1.7
L-glutamate
-
mutant T323A, pH 8.0, 37°C
1.8
L-glutamate
-
pH 8.2, 37°C
1.9
L-glutamate
holoenzyme
2.8
L-glutamate
pH 8.0, 15°C, recombinant enzyme
3.2
L-glutamate
heavy subunit
3.5
L-glutamate
-
recombinant catalytic subunit, pH 8.0, 37°C
3.76
L-glutamate
pH 7.5, 25°C, mutant R248K
5.2
L-glutamate
-
mutant R179A, pH 8.0, 37°C
5.3
L-glutamate
-
pH 8.2, 25°C
6.1
L-glutamate
pH 7.5, 25°C, mutant T117S
11
L-glutamate
-
mutant E93A, pH 8.0, 37°C, in presence of Mg2+
11
L-glutamate
pH 8.5, 40°C, recombinant His-tagged enzyme
12
L-glutamate
pH 8.5, 40°C, recombinant His-tagged enzyme
15.2
L-glutamate
pH 7.5, 25°C, mutant H121A
18.2
L-glutamate
-
catalytic subunit
18.2
L-glutamate
heavy subunit
130
L-glutamate
-
mutant R366A, pH 8.0, 37°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics for the wild-type and mutant enzymes
-
additional information
additional information
kinetics, kinetic mechanism
-
additional information
additional information
kinetics, kinetic mechanism
-
additional information
additional information
-
kinetics, recombinant enzyme
-
additional information
additional information
kinetics, recombinant enzyme
-
additional information
additional information
-
kinetics, wild-type enzyme and mutant C319A
-
additional information
additional information
Km values for diverse substrates in presence of Mg2+, or Mn2+, or both, kinetics
-
additional information
additional information
-
Km values for diverse substrates in presence of Mg2+, or Mn2+, or both, kinetics
-
additional information
additional information
preliminary steady state kinetics
-
additional information
additional information
-
preliminary steady state kinetics
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
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evolution
-
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
evolution
the enzyme encoded by GSH1 belongs to the eu-GC superfamily
malfunction
-
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
-
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
a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH
malfunction
GSH can be depleted through the specific downregulation of the GCL levels by hammerhead ribozyme
malfunction
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
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
-
a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH
-
metabolism
-
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
-
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
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
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
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
the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
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
the enzyme catalyzes the first step in the glutathione biosynthesis
metabolism
the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine
metabolism
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
-
the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus
-
metabolism
-
the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine
-
metabolism
-
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
-
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
-
physiological function
-
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
the enzyme is rate-limiting for glutathione synthesis
physiological function
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
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
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
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
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
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
the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 activity
physiological function
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
-
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
-
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
-
the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 activity
-
physiological function
-
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
-
additional information
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
-
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
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
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
-
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
-
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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?
x * 49300, catalytic subunit
?
-
x * 72000 + x * 32000, denaturing SDS-PAGE
?
-
x * 73000, calculation from nucleotide sequence
?
x * 74200, amino acid sequence calculation
?
-
x * 30548, calculation from nucleotide sequence
?
-
unlike kidney enzyme, most of liver enzyme is in a reduced form which does not have disulfide linkage between heavy and light chain
?
x * 90500, about, sequence calculation
?
-
x * 90500, about, sequence calculation
-
?
x * 78300, catalytic subunit
?
x * 71400, catalytic subunit
dimer
-
GCL reveals two redox-sensitive intramolecular disulfide bonds, CC1 and CC2, located at the homodimer interface that regulate plant GCL activity
dimer
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
-
1 * 80000, about, catalytic subunit, + 1 * 28000, about, modifier subunit, SDS-PAGE
dimer
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
dimer
-
1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
-
2 * 75000, recombinant wild-type and mutant enzymes, SDS-PAGE
dimer
-
heavy and light subunit
dimer
-
heterodimer of a catalytic subunit and a regulatory subunit, encoded by 2 genes
dimer
-
1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
-
heterodimer consisting of subunits GCLC and GCLM
dimer
-
the enzyme consists of a catalytic subunit GCLC and a modifier subunit GCLM
dimer
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
dimer
-
1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
-
heterodimer, comprising a catalytic subunit (GCLC) and a regulatory subunit (GCLM). GCLC alone can catalyze the formation of L-gamma-glutamyl-L-cysteine, its binding with GCLM enhances the enzyme activity by lowering the Km for glutamate and ATP, and increasing the Ki for GSH inhibition
dimer
-
1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
-
GCL is composed of catalytic GCLC and modifier GCLM subunits
dimer
-
heterodimer consisting of catalytic and modifier subunits GCLC and GCLM
dimer
-
2 * 34000, SDS-PAGE
dimer
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, amino acids contributing to the homodimer interface in GCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs. NtGCL forms a homodimer under oxidizing conditions
dimer
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
-
2 * 85000, SDS-PAGE
dimer
-
2 *85000, SDS-PAGE
dimer
-
1 * 66000 + 1 * 57000, SDS-PAGE
dimer
-
1 * 75000 + 1 * 25000, denaturing PAGE in presence of 50 mM DTT
dimer
-
1 * 75000 + 1 * 25000, nondenaturing PAGE in presence of 50 mM DTT
dimer
-
1 * 74000 + 1 * 24000, SDS-PAGE. One enzyme species of MW 100000 Da detected by SDS-PAGE after cross-linking with dimethylsuberimidate
dimer
-
1 * 73000 + 1 * 27700, PAGE in presence of 50 mM DTT
dimer
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
dimer
-
1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
-
heavy and light subunit
dimer
-
glutamatecysteine ligase is a heterodimer of a GCLC (GCL catalytic subunit) that possesses all of the enzymatic activity and a GCLM (GCL modifier subunit) that alters the Ki of GCLC for GSH. Differential regulation of glutamatecysteine ligase subunit expression and increased holoenzyme formation in response to cysteine deprivation
dimer
-
1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
heterodimer
1 * 74760, catalytic subunit, + 1 * 28510, regulatory subunit, sequence calculation
heterodimer
enzyme GCL is a heterodimeric enzyme consisting of a catalytic subunit (GCLc) and a modulatory subunit (GCLm), which are encoded by two genes. The catalytic subunit GCLc performs all the enzymatic activity and its catalytic efficiency is increased by the covalent interaction with the regulatory subunit GCLm
heterodimer
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
heterodimer
-
glutamate-cysteine ligase consists of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
heterodimer
glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modulator subunit (GCLM)
heterodimer
enzyme GCL is a heterodimeric enzyme consisting of a catalytic subunit (GCLc) and a modulatory subunit (GCLm), which are encoded by two genes
monomer
-
proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview
monomer
1 * 59900, catalytic unit
monomer
-
x * 35000, mutant enzyme modifier subunit, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
-
monomer
1 * 78100, catalytic unit
monomer
-
1 * 60000, about
monomer
1 * 58000, SDS-PAGE, 1 * 57663, mass spectrometry and sequence calculation
monomer
-
1 * 58000, SDS-PAGE, 1 * 57663, mass spectrometry and sequence calculation
-
monomer
-
bifunctional enzyme accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities
monomer
1 * 46000, recombinant enzyme, SDS-PAGE
monomer
1 * 77500, catalytic unit
monomer
-
proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview
additional information
glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
additional information
-
glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
additional information
-
quaternary structure
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. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
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. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
additional information
-
enzyme is build of 2 subunits, a modifier and a catalytic subunit, the modifier subunit DmGCLM possesses cysteine residues, Cyys213, Cys214, and Cys267, which can form covalent interactions with the catalytic subunit DmGCLC and modify its activity, the activity of the holoenzyme is enhanced compared to the catalytic subunit alone
additional information
-
enzyme consists of 2 subunits, the heavy catalytic one and the light regulatory one
additional information
-
enzyme consists of a catalytic GCLC and a modulatory GCLM subunit
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
-
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
-
reaction can be performed by the catalytic subunit alone, but presence of the regulatory subunit in the holoenzyme increases the activity
additional information
-
reaction can be performed by the catalytic subunit alone, but presence of the regulatory subunit in the holoenzyme increases the activity and the specificity with L-2-aminobutyrate as substrate
additional information
-
the holoenzyme consists of a heavy catalytic and a light modifier subunit, i.e. gamma-GCSH and gamma-GCSL, protein modeling
additional information
-
the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
-
GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
-
upon oxidative stress, activation of GCL occurrs within min of treatment and without any change in GCL protein levels, and coincides with an increase in the proportion of GCL catalytic subunit in the holoenzyme form. Likewise, GCL modifier subunit shifts from the monomeric form to holoenzyme and higher molecular weight species. Neither GCL activation, nor the formation of holoenzyme, requires a covalent intermolecular disulfide bridge between GCL catalytic subunit and GCL modifier subunit
additional information
-
the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
additional information
quarternary structure
additional information
quarternary structure
additional information
quaternary structure
additional information
quaternary structure
additional information
-
the dimeric enzyme is composed of a heavy, catalytic subunit and a light, regulatory subunit
additional information
-
the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
-
reaction is catalyzed by the catalytic subunit GCLC or by the holoenzyme (GCLholo), which comprises GCLC and the modifier subunit GCLM. GCLM decreases the Km for ATP by about 6fold and decreases the Km-value for glutamate and increases the Ki-value for feedback inhibition by GSH. GCLM increases by 4.4fold the turnover number for gamma-glutamylcysteine synthesis
additional information
-
reaction is catalyzed by the catalytic subunit GCLC or by the holoenzyme (GCLholo), which comprises GCLC and the modifier subunit GCLM. GCLM decreases the Km for ATP by about 6fold and decreases the Km-value for glutamate and increases the Ki-value for feedback inhibition by GSH. GCLM increases by 4.4fold the turnover number for gamma-glutamylcysteine synthesis
additional information
-
GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
-
the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
-
quarternary structure
additional information
three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
additional information
-
three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
-
additional information
-
the light subunit has a regulatory function affecting the affinity for Glu and GSH
additional information
-
the heavy subunit contains all of the structural requirements for enzymatic activity and also for feedback inhibition by glutathione
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
-
the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
-
GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
-
the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
-
the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
-
additional information
enzyme secondary structure analysis
additional information
-
enzyme secondary structure analysis
additional information
secondary structure analysis, overview
additional information
-
secondary structure analysis, overview
additional information
-
enzyme secondary structure analysis
-
additional information
-
secondary structure analysis, overview
-
additional information
-
quaternary structure
additional information
-
structure modeling
additional information
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
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C186S
-
mutation decreases activity by 20fold and abrogates the response to changes in redox environment
C349S
-
mutation reduces reaction rate by twofold
C364S
-
mutation reduces reaction rate by twofold
C406S
-
mutation decreases activity by 20fold and abrogates the response to changes in redox environment
DELTA1-85
mutant lacking the N-terminal localization sequence
C356A
the mutant shows reduced inhibition by DTT, but increased inhibition by glutathione
C139S/C267S
-
sequential site-directed mutagenesis, exchange of cysteine residues in the modifier subunit, the cysteine residues seem not to be involved in intersubunit disulfide bonding
C213S/C214S/C267S
-
sequential site-directed mutagenesis, exchange of cysteine residues in the modifier subunit, which can still associate with the catalytic subunit, but no longer form intersubunit disulfides, the enzyme activity is reduced but still higher than the activity of the catalytic subunit alone, the mutant is more sensitive to inhibition by GSH, human modifier subunit can complement the defect, the mutant strain shows a reduced GSH level
A494G
-
site-specific mutagenesis, 53% increased activity compared to wild-type enzyme
A494L
-
site-specific mutagenesis, 65% increased activity compared to wild-type enzyme
A494V
-
site-specific mutagenesis, 66% increased activity compared to wild-type enzyme
C 164S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S
-
site-directed mutagenesis, inactive mutant
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
-
site-directed mutagenesis, no complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395Y
-
site-directed mutagenesis, no complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q
-
site-directed mutagenesis, no complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195, the mutant enzyme lacking cysteine residues shows a decreased in vivo half-life
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395W
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372F/C395S
-
site-directed mutagenesis, no complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372F/S395C
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372W/S395C
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/V375F
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C372S/C433S/C439S
-
site-directed mutagenesis, no complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C357S/C433S/C439S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C106S/C164S/C205S/C223S/C433S/C439S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C164S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
C433S/C439S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
H150A
-
mutant enzyme His150Ala without enzymatic activity
S495T
-
site-specific mutagenesis, 62% increased activity compared to wild-type enzyme
C106S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
-
C164S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
-
C205S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
-
C223S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
-
H150A
-
mutant enzyme His150Ala without enzymatic activity
-
C248G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
C249G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, reduced activity of the holoenzyme compared to the wild-type enzyme
C295G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
C491G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
C501G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
C52G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
C553G
-
site-directed mutagenesis in the catalytic subunit, slightly reduced activity of the catalytic subunit, about 3.5fold reduced activity of the holoenzyme compared to the wild-type enzyme
C605G
-
site-directed mutagenesis in the catalytic subunit, reduced activity of the catalytic subunit, activity of the holoenzyme is similar to the wild-type enzyme
H370L
-
clinically relevant mutation in catalytic subunit GCLC. Significantly lower levels of glutathione relative to that of the wild type. Compromised enzymatic activity can largely be rescued by the addition of GCLM
P158L
-
clinically relevant mutation in catalytic subunit GCLC. Significantly lower levels of glutathione relative to that of the wild type, kinetic constants comparable to those of wild-type GCLC
P414L
-
clinically relevant mutation in catalytic subunit GCLC. Significantly lower levels of glutathione relative to that of the wild type, most compromised mutant among those studied. Compromised enzymatic activity can largely be rescued by the addition of GCLM
P462S
-
non-synonymous polymorphism in the gene encoding the catalytic subunit of glutamate-cysteine ligase. The polymorphism is present only in individuals of African descent and encodes an enzyme with significantly decreased in vitro activity when expressed by either a bacterial or mammalian cell expression system. Overexpression of the P462 wild-type GCLC enzyme results in higher intracellular glutathione concentrations than overexpression of the P462S isoform. Apoptotically stimulated mammalian cells overexpressing the P462S enzyme have increased caspase activation and increased DNA laddering compared to cells overexpressing the wild-type enzyme. The P462S polymorphism is in Hardy-Weinberg disequilibrium, with no individuals homozygous for the P462S polymorphism identified
C248A/C249A
-
mutant enzyme shows the same strength of binding to regulatory subunit (GCLM) as does wild-type GCLC, yet the catalytic activity is dramatically decreased
E103A
-
transduction of Hepa-1c1c7 cells with a catalytically inactive GCL catalytic subunit E103A mutant decreases cellular GCL activity in a dose-dependent manner
P158L
-
mutant enzyme shows the same strength of binding to regulatory subunit (GCLM) as does wild-type GCLC, yet the catalytic activity is dramatically decreased
H150A
site-directed mutagenesis, inactive mutant
K38A
-
mutant enzyme Lys38Arg: small changes in the catalytic properties, mutant enzyme K38N and K38E show marked decrease in enzymatic activity and about 2fold increase in Km for Glu
K38N
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
K38Q
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
K38R
site-directed mutagenesis, slightly decreased activity
C266A
about 2fold increase in both Km and Ki value
C266S
about 2fold increase in both Km and Ki value
D520stop
-
KM-value for L-Glu is 1.3fold higher than wild-type value, KM-values for L-Cys and ATP are nearly identical to wild-type value, Ki-value for GSH is 2.2fold higher than wild-type value, Ki-value for gamma-glutamylcysteine is 1.3fold higher than wild-type value
E494stop
-
KM-value for L-Glu, L-Cys and ATP are nearly identical to wild-type value, Ki-value for GSH is 7.7fold lower than wild-type value, Ki-value for gamma-glutamylcysteine is 2.4fold higher than wild-type value
G441stop
-
KM-value for L-Glu is 3.5fold higher than wild-type value, KM-values for L-Cys and ATP are nearly identical to wild-type value
H144A
-
KM-value for L-Glu is 10fold higher than wild-type value, KM-value for L-Cys is 6.4fold higher than wild-type value, KM-value for ATP is nearly identical to wild-type value
K526A
-
KM-value for L-Glu, L-Cys and ATP are nearly identical to wild-type value
R508stop
-
KM-value for L-Glu is 1.6fold higher than wild-type value, KM-value for L-Cys is 1.7fold higher than wild-type value, KM-value for ATP is nearly identical to wild-type value, Ki-value for GSH is 2fold higher than wild-type value, Ki-value for gamma-glutamylcysteine is 3.3fold higher than wild-type value
Y464stop
-
KM-values for L-Glu, L-Cys and ATP are nearly identical to wild-type value, Ki-value for GSH is 11fold lower than wild-type value, Ki-value for gamma-glutamylcysteine is 1.3fold lower than wild-type value
E37Q
site-directed mutagenesis, inactive mutant
E44Q
site-directed mutagenesis, inactive mutant
H121A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
H121Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R167A
site-directed mutagenesis, inactive mutant
R167K
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R248A
site-directed mutagenesis, inactive mutant
R248K
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
T117A
site-directed mutagenesis, inactive mutant
T117S
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E100A
-
site-directed mutagenesis, n1 metal binding site mutant, inactive mutant
E489A
-
site-directed mutagenesis, n2 metal binding site mutant, reduced activity
E53A
-
site-directed mutagenesis, n2 metal binding site mutant, reduced activity
E55A
-
site-directed mutagenesis, n1 metal binding site mutant, inactive mutant
E93A
-
site-directed mutagenesis, n1 metal binding site mutant, only capable of catalyzing L-Glu-dependent ATP hydrolysis and not the ligation between L-Glu and L-alpha-aminobutyrate
Q321A
-
site-directed mutagenesis, n2 metal binding site mutant, reduced activity
R179A
-
site-directed PCR-based mutagenesis, conserved residue, gamma-aminobutyrate-binding determinant, increase of Km for both L-Cys and L-Glu
R366A
-
site-directed PCR-based mutagenesis, mutant is active with gamma-aminobutyrate, increase of dissociation constant for L-Glu by 160fold, elimination of positive cooperativity of binding of L-Glu and ATP, interacts with the alpha-carboxylate of L-Glu, 220fold increase in Ki for GSH
R474A
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site-directed PCR-based mutagenesis, R474 is an ATP binding determinant, increase of Km for ATP by 20-100fold
R487A
-
site-directed PCR-based mutagenesis, R487 is an ATP binding determinant, increase of Km for ATP by 20-100fold
R491A
-
site-directed PCR-based mutagenesis, decrease of kcat for ATP hydrolysis
T323A
-
site-directed PCR-based mutagenesis, T323 is an alpha-phosphate of ATP binding determinant, increase of Km for ATP by 20-100fold
C106S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
C106S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C205S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
C205S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
C223S
-
site-directed mutagenesis, exchange of surface exposed cysteine residue for improved crystallization
C223S
-
site-directed mutagenesis, complementation of the gcs yeast mutant strain ABC 1195
R127C
-
naturally occuring mutation in patients with hemolytic anemia resulting from low erythrocyte enzyme levels, fibroblast cells from these patients bearing the mutation show 95% reduced enzyme activity and lowered Km for glutamate and aminobutyrate, as well as an increased Ki for GSH
R127C
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clinically relevant mutation in catalytic subunit GCLC. Significantly lower levels of glutathione relative to that of the wild type. Compromised enzymatic activity can largely be rescued by the addition of GCLM
C319A
-
mutant is insensitive to cystamine, but the catalytic efficiency, the kinetic mechanism, or the substrate affinities remain unaltered
C319A
-
site-directed mutagenesis, loss of sensitivity against cysteamine inactivation
additional information
-
mutation of Cys102, Cys251, Cys349, or Cys364 does not alter the response to redox environment
additional information
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
additional information
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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
additional information
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construction of a quadruple mutant of the enzyme termed gamma-GCS4CS
additional information
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natural K-12 mutant B possesses a Gly at position 494 compared to Ala for the K-12 wild-type enzyme, the initiation codon exchange mutant shows increased activity
additional information
overexpression of Escherichia coli gamma-glutamylcysteine synthetase in the cytosol of Populus tremula x Populus alba produces higher glutathione (GSH) concentrations in leaves, thereby indicating the potential for cadmium (Cd) phytoremediation. Analysis of net Cd2+ influx in association with H+/Ca2+, Cd tolerance, and the underlying molecular and physiological mechanisms, overview. Transgenic plants have higher Cd2+ uptake rates and elevated transcript levels of several genes involved in Cd2+ transport and detoxification compared with wild-type poplar plants. Transgenic plants exhibit greater Cd2+ accumulation in the aerial parts than wild-type plants in response to Cd2+ exposure. Transgenic poplars show lower concentrations of superoxide anions and H2O2, higher concentrations of total thiols, GSH and oxidized GSH in roots and/or leaves, and stimulated foliar GSH reductase activity compared with wild-type plants. The transgenic plants are more tolerant of 0.1 mM Cd2+ than wild-type plants, probably due to the GSH-mediated induction of the transcription of genes involved in Cd2+ transport and detoxification
additional information
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construction of a quadruple mutant of the enzyme termed gamma-GCS4CS
-
additional information
mutational analysis of the 5'-flanking sequence of the heavy subunit, site-directed mutagenesis
additional information
mutational analysis of the 5'-flanking sequence of the heavy subunit, site-directed mutagenesis
additional information
-
mutational analysis of the 5'-flanking sequence of the heavy subunit, site-directed mutagenesis
additional information
-
a GAG-repeat polymorphism in the 5'-UTR of the gene coding for the catalytic subunit, GCLC, is associated with altered GSH levels in vitro and in vivo
additional information
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GCLC and GCLM polymorphisms increase disease susceptibility in humans, overview
additional information
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GCLC polymorphisms are associated with lower lung function levels causing lung disease, especially in association with oxidative stress due to smoking
additional information
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the presence of at least one T allele in the -129 C/T polymorphism of the GCL catalytic subunit gene is independently associated with non-alcoholic steatohepatitis
additional information
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deletion analysis indicats that most regions, except a portion of the C-terminal region of catalytic subunit (GCLC) and a portion of the N-terminal region of regulatory subunit (GCLM), are required for the interaction to occur
additional information
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construction of Gclc and Gclm transgenic mice designed to conditionally overexpress GCL in the liver, conditional Gcl transgene expression in these mice promotes resistance to acetaminophen-induced liver injury
additional information
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transgenic mice that conditionally overexpress GCL subunits are protected from acetaminophen induced liver injury. Gclm null mice exhibit low GSH levels and enhanced sensitivity to acetaminophen. When Gclm expression and GCL activity are restored in Gclm conditional transgenic X Gclm null mice, they become resistant to APAP-induced liver damage. Construction of transgenic mouse models of inducible GCL subunit expression in the liver, overview
additional information
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a protein transduction approach whereby recombinant GCL protein can be rapidly and directly transferred into cells when coupled to the HIV TAT protein transduction domain. The TAT-GCL fusion proteins are capable of heterodimerization and formation of functional GCL holoenzyme in vitro. Exposure of Hepa-1c1c7 cells to the TAT-GCL fusion proteins results in the time- and dose-dependent transduction of both GCL subunits and increased cellular GCL activity and glutathione levels. A heterodimerization-competent, enzymatically deficient GCLC-TAT mutant was also generated in an attempt to create a dominant-negative suppressor of GCL
additional information
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construction of transgenic poplar plants expressing the bacterial enzyme in the cytosol and chloroplasts, transgenic plants show increased enzyme expression and induction, as well as increased detoxification activity and less phytootxic effects by the herbcides, overview
additional information
deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
additional information
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deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
additional information
generation of an GSH1 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
additional information
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generation of an GSH1 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
additional information
-
deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
-
additional information
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generation of an GSH1 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
-
additional information
-
mutants with a deletion of GSH1 cannot grow, a high level expression from a plasmid of the enzyme can compensate for adeletion of gene GSH2 encoding glutathione synthatase, the enzyme catalyzing the second step of glutathione biosynthesis
additional information
mutation of yAP-1 consensus sequence inhibits binding of yAP-1 protein, rendering the GSH1 promotor nonresponsive to exogenously expressed yAP-1
additional information
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wild-type enzyme is nearly uninhibited by GSH, shorter gamma-glutamylcysteine synthetase domain constructs are strongly inhibited. Chimeras of Streptococcus agalactiae gamma-glutamylcysteine synthetase-glutathione synthetase are made containing gamma-glutamylcysteine synthetase domain flexible loop sequences from Enterococcus faecalis and Pasteurella multocida gamma-glutamylcysteine synthetase-glutathione synthetase isoforms that are inhibited by GSH. Inhibition remains Streptococcus agalactiae-like (very weak)
additional information
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus
additional information
Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus
-
additional information
a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview
additional information
-
a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview
additional information
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
additional information
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
additional information
to convert feather hydrolysates into GSH with high values, the bifunctional glutathione synthetase, that comprises the activities of EC 6.3.2.2 and EC 6.3.2.3, encoded by gcsgs from Streptococcus thermophilus is surface displayed on Saccharomyces cerevisiae strain EBY100, the potential in glutathione (GSH) production from feather hydrolysates is analyzed. The surface-displayed GCSGS can be used to convert feather hydrolysates into GSH. 10 g/l of feather are converted into 321.8 mg/l GSH by the Trichoderma atroviride F6, with feather degrading ability, and surface-displayed GCSGS. Method optimization, overview
additional information
-
to convert feather hydrolysates into GSH with high values, the bifunctional glutathione synthetase, that comprises the activities of EC 6.3.2.2 and EC 6.3.2.3, encoded by gcsgs from Streptococcus thermophilus is surface displayed on Saccharomyces cerevisiae strain EBY100, the potential in glutathione (GSH) production from feather hydrolysates is analyzed. The surface-displayed GCSGS can be used to convert feather hydrolysates into GSH. 10 g/l of feather are converted into 321.8 mg/l GSH by the Trichoderma atroviride F6, with feather degrading ability, and surface-displayed GCSGS. Method optimization, overview
additional information
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
-
additional information
-
a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview
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a recombinant plasmid, pGMF, containing a gamma-glutamylcysteine synthetase gene (GSH-I) from Saccharomyces cerevisiae, is constructed with a copper-resistance gene as the selection marker and introduced into Saccharomyces cerevisiae YSF-31. The glutathione content of the recombinant strain is 1.5fold (13.1 mg/g*dry cells) of that in the host strain
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both regulatory subunit GCLM and catalytic subunit GCLC
catalytic subunit DNA sequence determination and analysis, expression as His-tagged wild-type enzyme and mutant R127C in Rosetta cells, functional expression of wild-type and mutant enzyme in enzyme-deficient cells
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cDNA for heavy subunit expressed in Escherichia coli
-
cloning and sequencing of the cDNA encoding the catalytic subunit
-
coexpression of the catalytic and the regulatory subunit from 2 different plasmids in Escherichia coli BL21(DE3), intracellular assembly of the holoenzyme
-
coexpression of the His-tagged catalytic and regulatory subunits in Spodoptera frugiperda Sf9 cells via baculovirus infection, formation of the holoenzyme in the cells
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DNA and amino acid sequence determination and analysis, single copy gene, genomic structure
DNA sequence determination and analysis
DNA sequence determination and analysis, 2 genes encode the 2 subunits, chromosomal mapping to 6p12 and 1p21, constitutive expression, expression of the heavy subunit alone or in combination with the light subunit in mammalian cells reveals that the regulatory subunit improves the activity, genetic regulation involving AP-1, overview, expression of several constructs in HepG2 cells, signaling for enzyme expression
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DNA sequence determination and analysis, gene Gsc1, expression in and functional complementation of an enzyme-deficient mutant strain
DNA sequence determination and analysis, gene GSH1 maps to chromosome X, expression in and functional complementation of an enzyme-deficient mutant strain, the yAP-1 responsive element in the promotor of gene GSH1 is involved in transcription of the gene in response to exposure to cadmium or hydrogen peroxide
DNA sequence determination and analysis, genetic regulation involving AP-1, overview
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DNA sequence determination and analysis, heavy and light subunits, overexpression of catalytic subunit and holoenzyme in Escherichia coli BL21(DE3)
DNA sequence determination and analysis, heterodimer of a catalytic subunit and a regulatory subunit, encoded by 2 genes: GLCLC for the catalytic subunit, and GLCLR for the regulatory subunit, GLCLC polymorphism and existence of 5 alleles as defined by the trinucleotide repeat, which exhibits a range of 4 to 10 uninterrupted repeat, genotyping for the repeat of 60 tumor cancer cell lines, overview
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DNA sequence determination and analysis, mapping to chromosome 6p12, heavy and light subunits, overexpression in Escherichia coli, individual or coexpression of the 2 subunits in COS cells, expression patterns, expression of several deletion mutants created fom the 5'-flanking region of the gene in human hepatoblastoma HepG2 cells, overexpression in human leukemia HL-60 cells
DNA sequence determination and analysis, mapping to chromosome 6p12, heavy and light subunits, overexpression in Escherichia coli, individual or coexpression of the 2 subunits in COS cells, expression patterns, expression of several deletion mutants created fom the 5'-flanking region of the gene in humen hepatoblastoma HepG2 cells, overexpression in human leukemia HL-60 cells
DNA sequence determination and analysis, mapping to chromosome 9, band D-E, heavy and light subunits
DNA sequence determination and analysis, overexpression in Escherichia coli
enzyme overexpression in Populus tremula x Populus alba (INRA female clone 717 1-B4) leaf cytosol, analysis of net Cd2+ influx in association with H+/Ca2+, Cd tolerance, and the underlying molecular and physiological mechanisms, overview
expresion of His-tagged wild-type subunits GCLM and GCLC and expression of His-tagged mutants in Escherichia coli BL21(DE3)
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expression as C-terminally His8-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3)
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expression in 293 and H4IIE cell lines
expression in Agrostis palustris
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expression in Escherichia coli
expression in Escherichia coli, 36-45% amino acid sequence identity with the enzymes from rat, human, Saccharomyces cerevisiae and Schizosaccharomyces pombe
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expression in Escherichia coli, transformation into tobacco plants
expression of a construct consisting of 3.8 kb of the enzyme's heavy subunit gene promotor in front of luciferase as well as a fragment of the 5'-flanking sequence, transient expression in COS-1 cells
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expression of both subunits in H4IIE cells via infection with adenovirus as a vector
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expression of the C-terminally His8-tagged wild-type enzyme in Escherichia coli BL21(DE3), expression of the mutant C319A in Escherichia coli BO265
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expression of the enzyme at high level in deletion mutant strains of GHS1 and GSH2, the latter encoding the glutathione synthetase, the GSH1 promotor is Met4-inducible and GSH repressible
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expression of the His-tagged wild-type enzyme and mutants in Spodoptera frugiperda Sf9 cells via baculovirus infection
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expression of wild-type and mutant C319A enzymes in Escherichia coli BL21(DE3) as His-tagged proteins
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expression of wild-type and mutant enzymes in Escherichia coli JM109
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expression of wild-type and mutants in Escherichia coli BL21(DE3) as C-terminally His-tagged proteins
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gene gclC encoding the catalytic subunit, DNA and amino acid sequence determination and analysis, quantitative expression analysis
gene GCLC, DNA and amino acid sequence determination and analysis, genotyping
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gene GCLC, semiquantitative expression analysis in endothelial cells
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gene gcsgs, recombinant functional enzyme expression on the cell surface of Saccharomyces cerevisiae strain EBY100, for cell surface expression, the gcsgs gene is fused with the 3'-end region of the alpha-agglutinin gene and cloned into plasmid YD1-GCSGS, recombinant expression in and secretion from Escherichia coli strain DH5alpha
gene GSH1 or GCL, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3)
gene GSH1, screening and DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21
gene gshA, DNA and amino acid sequence determination and analysis, promoter determination, and expression analysis by S1 mapping
gene gshA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene gshA, phylogenetic tree analysis of GCS lineage I, expression of C-terminally His-tagged wild-type and mutants in Escherichia coli strain BL21(DE3) or Origami from pTEF416, subcloning in Escherichia coli strain DH5alpha, complementation of Saccharomyces cerevisiae gsh deficient strain ABC1195
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gene gshA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gshF, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gshF, recombinant expression in Escherichia coli strain JM109 from plasmid pTrc99A
gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3) coexpressing Escherichia coli acetate kinase (gene ack)
gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3), coexpression with acetate kinase (gene ack) from Lactobacillus sanfranciscensis
gene gshF, recombinant expression in Saccharomyces cerevisiae strains BY4717 and BY-G from plasmid JMB125 leading to increased levels of glutathione
gene gshI with unusual initiation codon UUG, expression of wild-type and mutant enzymes in strain BH5262
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generation of C57Bl/6 mice that conditionally overexpress glutamate-cysteine ligase
genes gclc and gclcm (Ace-gclc and Ace-gclm), encoding the catalytic and the regulatory subunits, the genes are located on different chromosomes, DNA and amino acid sequence determination and analysis, sequence comparisons, real-time PCR analysis enzyme expression analysis, recombinant expression of the two subunits in Saccharomyces cerevisiae in the yeast two-hybrid system
genes gclC and gclM, DNA and amino acid sequence determination and analysis
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genes gclc and gclm, encoding the two different subunits, the different genes are located on separate chromosomes, quantitative RT-PCR enzyme expression analysis
genes GCLC and GCLM, expression analysis of the genes encoding both C and M subunits of GCL
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genes gclC and gclM, genotyping and expression analysis
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genes gclC and gclM, genotyping in healthy individuals and chronic obstructive pulmonary disease patients
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genes gclC and gclM, genotyping in healthy individuals and in schizophrenia patients, overview
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genes gclc and gclm, genotyping, analysis of correlation between genotype and smoking effects, overview
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genes GCLC and GCLM, quantitative RT-PCR expression analysis in biopsy samples from head and neck squamous cell carcinoma tissues and adjacent normal tissues
genes I79_010621 or Gclc and I79_022778 or Gclm, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR expression analysis of recombinant and wild-type enzyme subunits, determination of isozyme Gclc-X2 lacking the first 5 amino acids compared to isozymes Gclc-X0 and Gclc-X1, recombinant overexpression of the enzyme subunits in a CHO-T cell line Epi-CHO, derived from CHO-K1 cells. Gclc-X2 but not Gclm overexpression increases Gcl activity
genetic regulation involving AP-1, constitutive expression, overview
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Hepa-1 cells transfected with GCLC (catalytic subunit) and GCLM (modifier subunit) expression vectors
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nucleotide sequence is highly homologous to those of the enzymes of human liver, rat kidney and Saccharomyces cerevisiae
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partial DNA and amino acid sequence determination and analysis
the 2 subunits are encoded by 2 different genes and are located on chromosomes 9D-E and 3HI-3, genetic regulation involving AP-1, constitutive expression, overview
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the GAL4-UAS binary transgenic system is used to generate flies overexpressing either the catalytic (GCLc) or modulatory (GCLm) subunit of this enzyme, in a global or neuronally targeted pattern
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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
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transfecttion of embryonic fibroblast from GCLC null mice and expression in Saccharomyces cerevisiae
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wild-type and mutant enzymes are expressed in Escherichia coli
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both regulatory subunit GCLM and catalytic subunit GCLC
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both regulatory subunit GCLM and catalytic subunit GCLC
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DNA sequence determination and analysis
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DNA sequence determination and analysis
DNA sequence determination and analysis
DNA sequence determination and analysis
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
gene gshA, DNA and amino acid sequence determination and analysis, promoter determination, and expression analysis by S1 mapping
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gene gshA, DNA and amino acid sequence determination and analysis, promoter determination, and expression analysis by S1 mapping
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gene gshF, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gshF, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
generation of C57Bl/6 mice that conditionally overexpress glutamate-cysteine ligase
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generation of C57Bl/6 mice that conditionally overexpress glutamate-cysteine ligase
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