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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-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + alpha-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + D-Glu + L-alpha-aminobutyrate
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
-
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-alanine
ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
-
ir
ATP + L-Glu + beta-cyano-L-alanine
ADP + phosphate + gamma-L-Glu-beta-cyano-L-alanine
-
-
ir
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-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-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-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
-
-
ir
ATP + L-Glu + L-norvaline
ADP + phosphate + gamma-L-Glu-L-norvaline
-
-
ir
ATP + L-Glu + L-serine
ADP + phosphate + gamma-L-Glu-L-serine
-
-
ir
ATP + L-Glu + L-threonine
ADP + phosphate + gamma-L-Glu-L-threonine
-
-
ir
ATP + L-Glu + L-valine
ADP + phosphate + gamma-L-Glu-L-valine
-
-
ir
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-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
-
ir
ATP + 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 + butylamine
ADP + phosphate + N-butyl-L-glutamine
-
-
-
-
?
ATP + L-Glu + D-Cys
ADP + phosphate + gamma-L-Glu-D-Cys
-
-
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + N-ethyl-L-glutamine
-
-
-
-
?
ATP + L-Glu + L-2-aminobutanoate
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
ATP + L-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
ATP + L-Glu + L-Ser
ADP + phosphate + gamma-L-Glu-L-Ser
ATP + L-Glu + methylamine
ADP + phosphate + N-methyl-L-glutamine
-
-
-
-
?
ATP + L-Glu + n-propylamine
ADP + phosphate + N-propyl-L-glutamine
-
-
-
-
?
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-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
additional information
?
-
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 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-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-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
-
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-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-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
-
-
?
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
-
-
?
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-Glu + L-Cys
ADP + phosphate + gamma-L-Glu-L-Cys
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
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
-
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-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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-amino-4-[(2R,S)-2-carboxy-3-hydroxypropyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[(2R,S)-2-carboxy-3-phenylpropyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[(2R,S)-2-carboxybutyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[(2R,S)-2-carboxyhexyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[(2R,S)-2-carboxyoctyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[(2R,S)-2-carboxypropyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
(2S)-2-amino-4-[2-carboxyethyl-(R,S)-sulfonimidoyl]butanoic acid
-
-
L-buthionine-R-sulfoximine
-
L-buthionine-S-sulfoximine
L-buthionine-SR-sulfoximine
-
-
(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-Methylene glutamate
-
no inhibition
buthionine sulfoximine
-
only in presence of ATP
GSH
-
reduced, feedback inhibition of wild-type and mutants
L-buthionine-SR-sulfoximine
-
irreversible inactivation, ATP-dependent, a N-phosphorylated reaction intermediate is tightly bound to the enzyme, mechanism-based
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
S-sulfocysteine
-
no inhibition
S-sulfohomocysteine
-
no inhibition
Thiocholine disulfide
-
-
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
cystamine
-
-
cystamine
-
no inhibition
glutathione
-
feed-back inhibition
glutathione
-
GSH inhibits, GSSG has no inhibitory effect
additional information
no inhibition by cysteamine or slowly at high concentration
-
additional information
no inhibition by L-buthionine-R-sulfoximine
-
additional information
-
no inhibition by L-buthionine-R-sulfoximine
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.3
L-alpha-aminobutyrate
-
1.3 - 1.4
L-2-aminobutanoate
0.0001 - 0.00016
L-cysteine
0.0032 - 0.0053
L-glutamate
additional information
additional information
-
0.09
L-cysteine
strain B
0.5
L-glutamate
strain B
1.7
L-glutamate
strain KM
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
1.3
L-2-aminobutanoate
-
strain W
1.4
L-2-aminobutanoate
-
strain KM
0.09
L-Cys
-
-
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
0.5
L-Glu
-
-
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
-
-
24.2
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
27.2
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
28.7
ATP
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
30.1
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
30.5
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
39.7
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
46.9
ATP
-
pH 8.0, 25°C, wild-type enzyme
21.9
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
22.2
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
24.2
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
29.2
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
31.8
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
39.7
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
46.6
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme
22.1
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
22.7
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
23.8
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
30.4
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
31.2
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
31.4
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme
34
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
46.6
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
62.4
ATP
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
120.4
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
127.1
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
142.9
ATP
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
335
ATP
-
pH 8.0, 25°C, wild-type enzyme
397
ATP
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
172.9
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
198.8
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
199.1
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
222
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
288.6
L-cysteine
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
396.9
L-cysteine
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
466
L-cysteine
-
pH 8.0, 25°C, wild-type enzyme
4.3
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme, in presence of DTT
4.5
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT
6.9
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/S372C/S395Y
7.4
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/C372S/S395W
7.4
L-glutamate
-
pH 8.0, 25°C, mutant C106S/C164S/C205S/C223S/C357S/C372S/C395S/C433S/C439S/R374Q/V375F
8.1
L-glutamate
-
pH 8.0, 25°C, wild-type enzyme
8.5
L-glutamate
-
pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S
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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
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
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
-
construction of a quadruple mutant of the enzyme termed gamma-GCS4CS
additional information
-
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
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Huang, C.S.; Moore, W.R.; Meister, A.
On the active site thiol of gamma-glutamylcysteine synthetase: relationship to catalysis, inhibition, and regulation
Proc. Natl. Acad. Sci. USA
85
2464-2468
1988
Escherichia coli, Rattus norvegicus
brenda
Watanabe, K.; Murata, K.; Kimura, A.
Purification and characterization of gamma-glutamylcysteine synthetase of Escherichia coli B
Agric. Biol. Chem.
50
1925-1930
1986
Escherichia coli, Escherichia coli B / ATCC 11303
-
brenda
Kumagai, H.; Nakayama, R.; Tochikura, T.
gamma-Glutamylcysteine synthetase from Proteus mirabilis
Agric. Biol. Chem.
46
1301-1309
1982
Bacterium cadaveris, Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli Crooks, Escherichia coli FKU-1, Escherichia coli FKU-3, Escherichia coli FKU-8, Escherichia coli K-10, Escherichia coli S-96, Klebsiella aerogenes, Proteus mirabilis, Proteus vulgaris, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas schuylkilliensis
-
brenda
Murata, K.; Kimura, A.
Cloning of a gene responsible for the biosynthesis of glutathione in Escherichia coli B
Appl. Environ. Microbiol.
44
1444-1448
1982
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Inoue, Y.; Iba, Y.; Yano, H.; Murata, K.; Kimura, A.
Functional analysis of the gamma-glutamylcysteine synthetase of Escherichia coli B: effect of substitution of His-150 to Ala
Appl. Microbiol. Biotechnol.
38
473-477
1993
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Hibi, T.; Hisada, H.; Nakatsu, T.; Kato, H.; Oda, J.
Escherichia coli B gamma-glutamylcysteine synthetase: modification, purification, crystallization and preliminary crystallographic analysis
Acta Crystallogr. Sect. D
58
316-318
2002
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Griffith, O.W.; Mulcahy, R.T.
The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase
Adv. Enzymol. Relat. Areas Mol. Biol.
73
209-267
1999
Ascaris suum, Bos taurus, [Candida] boidinii, Ovis aries, Nicotiana tabacum, no activity in Entamoeba histolytica, Proteus mirabilis, Sus scrofa, Xenopus sp., no activity in Giardia sp., Mus musculus (A0A0H2UNM8), Mus musculus (P97494), Escherichia coli (P0A6W9), Rattus norvegicus (P19468), Rattus norvegicus (P48508), Saccharomyces cerevisiae (P32477), Arabidopsis thaliana (P46309), Homo sapiens (P48506), Homo sapiens (P48507), Homo sapiens, Leishmania tarentolae (P90557), Schizosaccharomyces pombe (Q09768), Trypanosoma brucei (Q26820), Acidithiobacillus ferrooxidans (Q56277)
brenda
Katoh, M.; Hiratake, J.; Oda, J.i.
ATP-dependent inactivation of Escherichia coli gamma-glutamylcysteine synthetase by L-glutamic acid gamma-monohydroxamate
Biosci. Biotechnol. Biochem.
62
1455-1457
1998
Escherichia coli
brenda
Hiratake, J.; Irie, T.; Tokutake, N.; Oda, J.i.
Recognition of a cysteine substrate by E. coli gamma-glutamylcysteine synthetase probed by sulfoximine-based transition-state analogue inhibitors
Biosci. Biotechnol. Biochem.
66
1500-1514
2002
Escherichia coli
brenda
Kwak, J.H.; Nam, Y.S.; Lee, S.Y.
Site-specific mutagenesis of the gshI gene for increasing the activity of gamma-glutamylcysteine synthetase in Escherichia coli K-12
J. Biochem. Mol. Biol.
31
254-257
1998
Escherichia coli
-
brenda
Kelly, B.S.; Antholine, W.E.; Griffith, O.W.
Escherichia coli gamma-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding
J. Biol. Chem.
277
50-58
2002
Escherichia coli (P0A6W9), Escherichia coli, Escherichia coli JM109 (P0A6W9)
brenda
Hibi, T.; Nii, H.; Nakatsu, T.; Kimura, A.; Kato, H.; Hiratake, J.; Oda, J.
Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis
Proc. Natl. Acad. Sci. USA
101
15052-15057
2004
Escherichia coli
brenda
Miyake, K.; Kakita, S.
A novel catalytic ability of gamma-glutamylcysteine synthetase of Escherichia coli and its application in theanine production
Biosci. Biotechnol. Biochem.
73
2677-2683
2009
Escherichia coli
brenda
Herschbach, C.; Rizzini, L.; Mult, S.; Hartmann, T.; Busch, F.; Peuke, A.D.; Kopriva, S.; Ensminger, I.
Over-expression of bacterial gamma-glutamylcysteine synthetase (GSH1) in plastids affects photosynthesis, growth and sulphur metabolism in poplar (Populus tremula x Populus alba) dependent on the resulting gamma-glutamylcysteine and glutathione levels
Plant Cell Environ.
33
1138-1151
2010
Escherichia coli
brenda
Kumar, S.; Kasturia, N.; Sharma, A.; Datt, M.; Bachhawat, A.K.
Redox-dependent stability of the gamma-glutamylcysteine synthetase enzyme of Escherichia coli: a novel means of redox regulation
Biochem. J.
449
783-794
2013
Escherichia coli
brenda
He, J.; Li, H.; Ma, C.; Zhang, Y.; Polle, A.; Rennenberg, H.; Cheng, X.; Luo, Z.B.
Overexpression of bacterial gamma-glutamylcysteine synthetase mediates changes in cadmium influx, allocation and detoxification in poplar
New Phytol.
205
240-254
2015
Escherichia coli (P0A6W9)
brenda