BRENDA - Enzyme Database

The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase

Griffith, O.W.; Mulcahy, R.T.; Adv. Enzymol. Relat. Areas Mol. Biol. 73, 209-267 (1999) View publication on PubMed

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
6.3.2.2
H2O2
induction of enzyme expression, increase in activity in V79 cells independent on transcription level
Homo sapiens
6.3.2.2
H2O2
induction of in enzyme expression and activity
Saccharomyces cerevisiae
Application
EC Number
Application
Commentary
Organism
6.3.2.2
medicine
enzyme inhibitor L-buthionine-S-sulfoximine is used to modulate GSH levels in cancer patients, overview
Homo sapiens
Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
6.3.2.2
DNA sequence determination and analysis
[Candida] boidinii
6.3.2.2
DNA sequence determination and analysis
Escherichia coli
6.3.2.2
DNA sequence determination and analysis
Arabidopsis thaliana
6.3.2.2
DNA sequence determination and analysis
Leishmania tarentolae
6.3.2.2
DNA sequence determination and analysis, gene Gsc1, expression in and functional complementation of an enzyme-deficient mutant strain
Schizosaccharomyces pombe
6.3.2.2
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
Saccharomyces cerevisiae
6.3.2.2
DNA sequence determination and analysis, heavy and light subunits, overexpression of catalytic subunit and holoenzyme in Escherichia coli BL21(DE3)
Rattus norvegicus
6.3.2.2
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
Homo sapiens
6.3.2.2
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
Homo sapiens
6.3.2.2
DNA sequence determination and analysis, mapping to chromosome 9, band D-E, heavy and light subunits
Mus musculus
6.3.2.2
DNA sequence determination and analysis, overexpression in Escherichia coli
Trypanosoma brucei
Engineering
EC Number
Protein Variants
Commentary
Organism
6.3.2.2
H150A
site-directed mutagenesis, inactive mutant
Rattus norvegicus
6.3.2.2
K38N
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
Rattus norvegicus
6.3.2.2
K38Q
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
Rattus norvegicus
6.3.2.2
K38R
site-directed mutagenesis, slightly decreased activity
Rattus norvegicus
6.3.2.2
additional information
mutation of yAP-1 consensus sequence inhibits binding of yAP-1 protein, rendering the GSH1 promotor nonresponsive to exogenously expressed yAP-1
Saccharomyces cerevisiae
6.3.2.2
additional information
mutational analysis of the 5'-flanking sequence of the heavy subunit, site-directed mutagenesis
Homo sapiens
General Stability
EC Number
General Stability
Organism
6.3.2.2
enzyme is inactivated by freezing
Sus scrofa
6.3.2.2
enzyme is inactivated by freezing
Bos taurus
6.3.2.2
enzyme is inactivated by freezing
Ovis aries
6.3.2.2
enzyme is inactivated by freezing
Proteus mirabilis
6.3.2.2
enzyme is inactivated by freezing
[Candida] boidinii
6.3.2.2
enzyme is inactivated by freezing
Mus musculus
6.3.2.2
enzyme is inactivated by freezing
Homo sapiens
6.3.2.2
enzyme is inactivated by freezing
Rattus norvegicus
6.3.2.2
glycerol is required for enzyme stability during storage
Homo sapiens
6.3.2.2
glycerol is required for enzyme stability during storage
Rattus norvegicus
6.3.2.2
inactivated by freezing
Mus musculus
6.3.2.2
L-glutamate stabilizes the enzyme during purification
Rattus norvegicus
6.3.2.2
L-glutamate stabilizes the enzyme during purification,
Homo sapiens
6.3.2.2
L-glutamate stabilizes the enzyme during purification,
Rattus norvegicus
6.3.2.2
Mn2+ destabilizes the enzyme during purification
Homo sapiens
6.3.2.2
Mn2+ destabilizes the enzyme during purification
Rattus norvegicus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
6.3.2.2
4-methylene-L-glutamate
weak, competitive
Rattus norvegicus
6.3.2.2
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
Rattus norvegicus
6.3.2.2
buthionine sulfone
-
Rattus norvegicus
6.3.2.2
buthionine sulfoximine
-
Arabidopsis thaliana
6.3.2.2
buthionine sulfoximine
-
Ascaris suum
6.3.2.2
buthionine sulfoximine
-
[Candida] boidinii
6.3.2.2
buthionine sulfoximine
-
Leishmania tarentolae
6.3.2.2
buthionine sulfoximine
-
Nicotiana tabacum
6.3.2.2
buthionine sulfoximine
-
Saccharomyces cerevisiae
6.3.2.2
buthionine sulfoximine
-
Schizosaccharomyces pombe
6.3.2.2
Chloroacetone
-
Rattus norvegicus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Bos taurus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Homo sapiens
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Mus musculus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Ovis aries
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Rattus norvegicus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Sus scrofa
6.3.2.2
D-3-amino-1-chloro-2-pentanone
-
Rattus norvegicus
6.3.2.2
gamma-methylene-D-glutamate
-
Rattus norvegicus
6.3.2.2
GSH
feedback inhibition
Ascaris suum
6.3.2.2
GSH
feedback inhibition
Bos taurus
6.3.2.2
GSH
feedback inhibition
[Candida] boidinii
6.3.2.2
GSH
feedback inhibition
Escherichia coli
6.3.2.2
GSH
feedback inhibition
Homo sapiens
6.3.2.2
GSH
feedback inhibition
Mus musculus
6.3.2.2
GSH
feedback inhibition
Nicotiana tabacum
6.3.2.2
GSH
feedback inhibition
Ovis aries
6.3.2.2
GSH
feedback inhibition, competitive to L-Glu
Rattus norvegicus
6.3.2.2
GSH
feedback inhibition
Sus scrofa
6.3.2.2
GSH
feedback inhibition
Trypanosoma brucei
6.3.2.2
iodoacetamide
-
Rattus norvegicus
6.3.2.2
L-buthionine sulfone
competitive, reversible
Rattus norvegicus
6.3.2.2
L-buthionine-R-sulfoximine
-
Escherichia coli
6.3.2.2
L-buthionine-R-sulfoximine
-
Homo sapiens
6.3.2.2
L-buthionine-R-sulfoximine
mechanism-based, competitive, reversible
Rattus norvegicus
6.3.2.2
L-buthionine-S-sulfoximine
strong inhibition
Escherichia coli
6.3.2.2
L-buthionine-S-sulfoximine
strong inhibition
Homo sapiens
6.3.2.2
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
Rattus norvegicus
6.3.2.2
methionine sulfoximine
-
Mus musculus
6.3.2.2
methionine sulfoximine
competitive and reversible
Rattus norvegicus
6.3.2.2
additional information
no inhibition by cysteamine or slowly at high concentration
Escherichia coli
6.3.2.2
additional information
no inhibition by alpha-ethyl-methionine sulfoximine
Mus musculus
6.3.2.2
additional information
inhibition mechanisms, no inhibition by L-homocysteine sulfonate
Rattus norvegicus
6.3.2.2
NO
-
Mus musculus
6.3.2.2
ophthalmic acid
-
Rattus norvegicus
6.3.2.2
S-butyl-DL-homocysteine-SR-sulfoximine
-
Mus musculus
6.3.2.2
S-butyl-DL-homocysteine-SR-sulfoximine
-
Rattus norvegicus
6.3.2.2
S-nitroso-L-cysteine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
Rattus norvegicus
6.3.2.2
S-nitroso-L-cysteinylglycine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
Rattus norvegicus
6.3.2.2
S-sulfo-homocysteine
-
Rattus norvegicus
6.3.2.2
S-sulfo-L-cysteine
-
Rattus norvegicus
6.3.2.2
Trinitrobenzene sulfonate
inactivates the enzyme
Rattus norvegicus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.3.2.2
additional information
-
additional information
kinetics, kinetic mechanism
Rattus norvegicus
6.3.2.2
0.09
-
L-cysteine
strain B
Escherichia coli
6.3.2.2
0.1
-
L-cysteine
strain W
Escherichia coli
6.3.2.2
0.1
-
ATP
strain B
Escherichia coli
6.3.2.2
0.1
-
L-cysteine
holoenzyme
Homo sapiens
6.3.2.2
0.13
-
L-cysteine
heavy subunit
Homo sapiens
6.3.2.2
0.15
-
L-cysteine
-
Proteus mirabilis
6.3.2.2
0.16
-
ATP
-
Proteus mirabilis
6.3.2.2
0.19
-
L-cysteine
-
Nicotiana tabacum
6.3.2.2
0.2
-
ATP
-
[Candida] boidinii
6.3.2.2
0.2
-
L-cysteine
strain KM
Escherichia coli
6.3.2.2
0.2
-
ATP
holoenzyme
Rattus norvegicus
6.3.2.2
0.2
-
L-cysteine
heavy subunit and holoenzyme
Rattus norvegicus
6.3.2.2
0.24
-
L-glutamate
-
Trypanosoma brucei
6.3.2.2
0.31
-
L-alpha-aminobutyrate
-
Ascaris suum
6.3.2.2
0.4
-
L-cysteine
-
[Candida] boidinii
6.3.2.2
0.4
-
ATP
holoenzyme
Homo sapiens
6.3.2.2
0.41
-
L-cysteine
-
Ascaris suum
6.3.2.2
0.5
-
L-glutamate
strain B
Escherichia coli
6.3.2.2
0.69
-
L-cysteine
-
Trypanosoma brucei
6.3.2.2
0.7
-
L-glutamate
strain W
Escherichia coli
6.3.2.2
0.71
-
ATP
-
Trypanosoma brucei
6.3.2.2
0.94
-
L-glutamate
-
Ascaris suum
6.3.2.2
1
-
L-alpha-aminobutyrate
-
Rattus norvegicus
6.3.2.2
1.3
-
L-alpha-aminobutyrate
-
Escherichia coli
6.3.2.2
1.4
-
L-glutamate
-
[Candida] boidinii
6.3.2.2
1.4
-
L-glutamate
holoenzyme
Rattus norvegicus
6.3.2.2
1.41
-
ATP
-
Ascaris suum
6.3.2.2
1.6
-
L-glutamate
-
Proteus mirabilis
6.3.2.2
1.7
-
L-glutamate
strain KM
Escherichia coli
6.3.2.2
1.9
-
L-glutamate
holoenzyme
Homo sapiens
6.3.2.2
2.3
-
L-alpha-aminobutyrate
-
Homo sapiens
6.3.2.2
3.2
-
L-glutamate
heavy subunit
Homo sapiens
6.3.2.2
7.3
-
(R)-beta-amino-iso-butyrate
-
Bos taurus
6.3.2.2
10.4
-
L-glutamate
-
Nicotiana tabacum
6.3.2.2
13.3
-
(S)-beta-amino-iso-butyrate
-
Bos taurus
6.3.2.2
18.2
-
L-glutamate
heavy subunit
Rattus norvegicus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
6.3.2.2
cytosol
exclusively
Sus scrofa
5829
-
6.3.2.2
cytosol
exclusively
Bos taurus
5829
-
6.3.2.2
cytosol
exclusively
Ovis aries
5829
-
6.3.2.2
cytosol
exclusively
Homo sapiens
5829
-
6.3.2.2
cytosol
exclusively
Rattus norvegicus
5829
-
6.3.2.2
cytosol
exclusively
Mus musculus
5829
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.3.2.2
Mg2+
required, bound to the erythrocyte enzyme
Homo sapiens
6.3.2.2
Mg2+
required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by 25%
Rattus norvegicus
6.3.2.2
Mg2+
required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by only 25%
Rattus norvegicus
6.3.2.2
Mn2+
bound to the erythrocyte enzyme
Homo sapiens
6.3.2.2
Mn2+
bound to the kidney enzyme, can substitute for Mg2+ by 25%
Rattus norvegicus
6.3.2.2
Mn2+
bound to the kidney enzyme, can substitute for Mg2+ by only 25%
Rattus norvegicus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
6.3.2.2
30500
-
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
30600
-
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
30700
-
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
34000
-
2 * 34000
Nicotiana tabacum
6.3.2.2
49300
-
x * 49300, catalytic subunit
Acidithiobacillus ferrooxidans
6.3.2.2
58200
-
1 * 58200
Escherichia coli
6.3.2.2
59900
-
1 * 59900, catalytic unit
Arabidopsis thaliana
6.3.2.2
60000
-
2 * 60000, SDS-PAGE
[Candida] boidinii
6.3.2.2
60000
-
1 * 60000, about
Proteus mirabilis
6.3.2.2
71400
-
x * 71400, catalytic subunit
Schizosaccharomyces pombe
6.3.2.2
72600
-
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
72700
-
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
72800
-
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
77500
-
1 * 77500, catalytic unit
Trypanosoma brucei
6.3.2.2
78100
-
1 * 78100, catalytic unit
Leishmania tarentolae
6.3.2.2
78300
-
x * 78300, catalytic subunit
Saccharomyces cerevisiae
6.3.2.2
100000
-
kidney enzyme, native PAGE
Rattus norvegicus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
6.3.2.2
ATP + L-Glu + L-Cys
Sus scrofa
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
Bos taurus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Ovis aries
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
Nicotiana tabacum
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
Proteus mirabilis
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
Ascaris suum
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
[Candida] boidinii
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
Xenopus sp.
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
Saccharomyces cerevisiae
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
Escherichia coli
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
Trypanosoma brucei
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
Arabidopsis thaliana
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
Acidithiobacillus ferrooxidans
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
Leishmania tarentolae
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
Schizosaccharomyces pombe
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
Rattus norvegicus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Mus musculus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Homo sapiens
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Homo sapiens
ir
6.3.2.2
additional information
Sus scrofa
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Sus scrofa
?
6.3.2.2
additional information
Bos taurus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Bos taurus
?
6.3.2.2
additional information
Ovis aries
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Ovis aries
?
6.3.2.2
additional information
Mus musculus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Mus musculus
?
6.3.2.2
additional information
Homo sapiens
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
?
-
Homo sapiens
?
6.3.2.2
additional information
Rattus norvegicus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
?
-
Rattus norvegicus
?
6.3.2.2
additional information
Trypanosoma brucei
most of the GSH produced in this pathway is converted to trypanothione
?
-
Trypanosoma brucei
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
6.3.2.2
Acidithiobacillus ferrooxidans
Q56277
-
-
6.3.2.2
Arabidopsis thaliana
P46309
-
-
6.3.2.2
Ascaris suum
-
-
-
6.3.2.2
Bos taurus
-
-
-
6.3.2.2
Escherichia coli
P0A6W9
strain W, strain B, strain KM
-
6.3.2.2
Homo sapiens
P48506
heavy, catalytic subunit
-
6.3.2.2
Homo sapiens
P48507
light, regulatory subunit
-
6.3.2.2
Leishmania tarentolae
P90557
-
-
6.3.2.2
Mus musculus
A0A0H2UNM8
light, regulatory subunit
-
6.3.2.2
Mus musculus
P97494
heavy, catalytic subunit
-
6.3.2.2
Nicotiana tabacum
-
-
-
6.3.2.2
no activity in Entamoeba histolytica
-
-
-
6.3.2.2
no activity in Giardia sp.
-
-
-
6.3.2.2
Ovis aries
-
-
-
6.3.2.2
Proteus mirabilis
-
-
-
6.3.2.2
Rattus norvegicus
P19468
heavy, catalytic subunit
-
6.3.2.2
Rattus norvegicus
P48508
light, regulatory subunit
-
6.3.2.2
Saccharomyces cerevisiae
P32477
-
-
6.3.2.2
Schizosaccharomyces pombe
Q09768
-
-
6.3.2.2
Sus scrofa
-
-
-
6.3.2.2
Trypanosoma brucei
Q26820
-
-
6.3.2.2
Xenopus sp.
-
-
-
6.3.2.2
[Candida] boidinii
-
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
6.3.2.2
phosphoprotein
the heavy, catalytic subunit can be phosphorylated by dibutyrl cAMP in hepatocytes, and by protein kinase C, protein kinase A, and Ca2+/calmodulin-dpendent kinas II on serine and threonine residues in presence of Mg2+, regulatory role of dephosphorylation/phosphorylation in vivo
Rattus norvegicus
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
6.3.2.2
-
Proteus mirabilis
6.3.2.2
-
Saccharomyces cerevisiae
6.3.2.2
-
Escherichia coli
6.3.2.2
from erythrocyte
Ovis aries
6.3.2.2
from erythrocyte, from malignant astrocytoma cell line, recombinant from Escherichia coli to homogeneity
Homo sapiens
6.3.2.2
from kidney, liver and erythrocytes, recombinant catalytic subunit and holoenzyme from Escherichia coli to homogeneity
Rattus norvegicus
6.3.2.2
from lens
Bos taurus
6.3.2.2
from liver
Sus scrofa
6.3.2.2
from liver
Xenopus sp.
6.3.2.2
from reproductive tissue
Ascaris suum
6.3.2.2
partially
Nicotiana tabacum
6.3.2.2
recombinant from Escherchia coli to homogeneity
Trypanosoma brucei
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, catalytic mechanism and substrate binding
Bos taurus
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, catalytic mechanism, active site and substrate binding, Lys38 is an active site residue in the glutamyl binding site, His150 is essential for activity
Rattus norvegicus
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
Sus scrofa
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
Ovis aries
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
Homo sapiens
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
enzyme-bound reaction intermediate is a gamma-glutamyl-phosphate, active site cysteine, mechanism
Mus musculus
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
no conserved cysteine residue in the active site
Escherichia coli
6.3.2.2
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
no conserved cysteine residue in the active site
Leishmania tarentolae
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
6.3.2.2
astrocytoma cell
malignant cell line
Homo sapiens
-
6.3.2.2
brain
-
Homo sapiens
-
6.3.2.2
brain
-
Rattus norvegicus
-
6.3.2.2
colon
-
Homo sapiens
-
6.3.2.2
erythrocyte
-
Ovis aries
-
6.3.2.2
erythrocyte
-
Homo sapiens
-
6.3.2.2
erythrocyte
-
Rattus norvegicus
-
6.3.2.2
heart
-
Homo sapiens
-
6.3.2.2
kidney
-
Sus scrofa
-
6.3.2.2
kidney
-
Bos taurus
-
6.3.2.2
kidney
-
Ovis aries
-
6.3.2.2
kidney
-
Homo sapiens
-
6.3.2.2
kidney
-
Rattus norvegicus
-
6.3.2.2
kidney
-
Mus musculus
-
6.3.2.2
lens
-
Bos taurus
-
6.3.2.2
liver
-
Sus scrofa
-
6.3.2.2
liver
-
Bos taurus
-
6.3.2.2
liver
-
Ovis aries
-
6.3.2.2
liver
-
Xenopus sp.
-
6.3.2.2
liver
-
Homo sapiens
-
6.3.2.2
liver
-
Rattus norvegicus
-
6.3.2.2
liver
-
Mus musculus
-
6.3.2.2
lung
-
Homo sapiens
-
6.3.2.2
macrophage
-
Mus musculus
-
6.3.2.2
additional information
expression patterns of both subunits in the tissues, overview, 2 transcript different in size for both the heavy and light subunit occur in the tissues, some tumors overexpress only the heavy subunit rather than the holoenzyme
Homo sapiens
-
6.3.2.2
additional information
expression patterns of both subunits in the tissues, overview, 2 transcripts different in size for both the heavy and light subunit occur in the tissues, some tumors overexpress only the heavy subunit rather than the holoenzyme
Homo sapiens
-
6.3.2.2
ovary
-
Homo sapiens
-
6.3.2.2
pancreas
-
Homo sapiens
-
6.3.2.2
peripheral blood
-
Homo sapiens
-
6.3.2.2
placenta
-
Homo sapiens
-
6.3.2.2
prostate
-
Homo sapiens
-
6.3.2.2
reproductive system
-
Ascaris suum
-
6.3.2.2
skeletal muscle
-
Homo sapiens
-
6.3.2.2
small intestine
-
Homo sapiens
-
6.3.2.2
spleen
-
Homo sapiens
-
6.3.2.2
testis
-
Homo sapiens
-
6.3.2.2
thymus
-
Homo sapiens
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
6.3.2.2
additional information
-
-
Rattus norvegicus
6.3.2.2
0.001
-
native COS cells
Homo sapiens
6.3.2.2
0.013
-
-
[Candida] boidinii
6.3.2.2
0.014
-
transformed COS cells expressing both the recombinant subunits at equal amounts
Homo sapiens
6.3.2.2
0.038
-
transformed COS cells expressing the recombinant catalytic subunit
Homo sapiens
6.3.2.2
25
-
purified enzyme
Rattus norvegicus
6.3.2.2
25
-
purified recombinant enzyme
Homo sapiens
Storage Stability
EC Number
Storage Stability
Organism
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Sus scrofa
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Bos taurus
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Ovis aries
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Homo sapiens
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Rattus norvegicus
6.3.2.2
-80°C, enzyme is very stable at
Escherichia coli
6.3.2.2
-80°C, enzyme is very stable at
Arabidopsis thaliana
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
6.3.2.2
ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + beta-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + beta-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + beta-methyl-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + beta-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + D-Glu + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-alpha-aminomethylglutarate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-alpha-aminomethylglutaryl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-alpha-aminomethylsuccinate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-alpha-aminomethylsuccinyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-beta-aminoadipate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-beta-aminoadipyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu
-
649263
Rattus norvegicus
ADP + phosphate + 5-oxoproline
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + (R)-beta-amino-iso-butyrate
2fold less reactive as the S-isomer
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-(R)-beta-amino-iso-butyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + (S)-beta-amino-iso-butyrate
2fold as reactive as the R-isomer
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-(S)-beta-amino-iso-butyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + beta-chloro-L-alanine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + DL-allylglycine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + DL-beta-amino-iso-butyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + Gly
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-Gly
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-2-aminobutanoate
-
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
?
6.3.2.2
ATP + L-Glu + L-alanine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alanine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminoheptanoate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alpha-aminoheptanoate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Sus scrofa
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Ovis aries
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Nicotiana tabacum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Proteus mirabilis
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
[Candida] boidinii
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Xenopus sp.
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Saccharomyces cerevisiae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Trypanosoma brucei
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Arabidopsis thaliana
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Acidithiobacillus ferrooxidans
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Leishmania tarentolae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Mus musculus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Schizosaccharomyces pombe
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Sus scrofa
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Ovis aries
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Nicotiana tabacum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Proteus mirabilis
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
[Candida] boidinii
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Xenopus sp.
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Saccharomyces cerevisiae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Trypanosoma brucei
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Arabidopsis thaliana
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Acidithiobacillus ferrooxidans
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Leishmania tarentolae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Schizosaccharomyces pombe
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Mus musculus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-homocysteine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-homoserine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-homoserine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-norleucine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-norleucine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-norvaline
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-norvaline
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-serine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-serine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-threonine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-threonine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-threonine
allo-L-threonine is a 5fold better substrate than L-threonine
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-threonine
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + S-methyl-L-cysteine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + threo-beta-hydroxy-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + threo-beta-hydroxy-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + threo-gamma-hydroxy-L-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + threo-gamma-hydroxy-L-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
additional information
substrate specificity
649263
Escherichia coli
?
-
649263
Escherichia coli
?
6.3.2.2
additional information
substrate specificity
649263
Homo sapiens
?
-
649263
Homo sapiens
?
6.3.2.2
additional information
substrate specificity, beta-alanine, (R,S)-beta-amino-n-butyrate, and (R,S)-alpha-ethyl-beta-alanine are no substrates
649263
Bos taurus
?
-
649263
Bos taurus
?
6.3.2.2
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
649263
Rattus norvegicus
?
-
649263
Rattus norvegicus
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Sus scrofa
?
-
649263
Sus scrofa
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Bos taurus
?
-
649263
Bos taurus
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Ovis aries
?
-
649263
Ovis aries
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Mus musculus
?
-
649263
Mus musculus
?
6.3.2.2
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
649263
Homo sapiens
?
-
649263
Homo sapiens
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
649263
Rattus norvegicus
?
-
649263
Rattus norvegicus
?
6.3.2.2
additional information
most of the GSH produced in this pathway is converted to trypanothione
649263
Trypanosoma brucei
?
-
649263
Trypanosoma brucei
?
Subunits
EC Number
Subunits
Commentary
Organism
6.3.2.2
?
x * 49300, catalytic subunit
Acidithiobacillus ferrooxidans
6.3.2.2
?
x * 71400, catalytic subunit
Schizosaccharomyces pombe
6.3.2.2
?
x * 78300, catalytic subunit
Saccharomyces cerevisiae
6.3.2.2
dimer
2 * 60000, SDS-PAGE
[Candida] boidinii
6.3.2.2
dimer
2 * 34000
Nicotiana tabacum
6.3.2.2
dimer
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
dimer
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
dimer
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
monomer
1 * 58200
Escherichia coli
6.3.2.2
monomer
1 * 59900, catalytic unit
Arabidopsis thaliana
6.3.2.2
monomer
1 * 60000, about
Proteus mirabilis
6.3.2.2
monomer
1 * 77500, catalytic unit
Trypanosoma brucei
6.3.2.2
monomer
1 * 78100, catalytic unit
Leishmania tarentolae
6.3.2.2
More
quarternary structure
Ovis aries
6.3.2.2
More
quarternary structure
Mus musculus
6.3.2.2
More
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
Rattus norvegicus
6.3.2.2
More
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
Homo sapiens
6.3.2.2
More
quaternary structure
Sus scrofa
6.3.2.2
More
quaternary structure
Bos taurus
6.3.2.2
More
quaternary structure
Mus musculus
6.3.2.2
More
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
Trypanosoma brucei
6.3.2.2
More
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
Leishmania tarentolae
Synonyms
EC Number
Synonyms
Commentary
Organism
6.3.2.2
gamma-GCS
-
Sus scrofa
6.3.2.2
gamma-GCS
-
Bos taurus
6.3.2.2
gamma-GCS
-
Ovis aries
6.3.2.2
gamma-GCS
-
Nicotiana tabacum
6.3.2.2
gamma-GCS
-
Proteus mirabilis
6.3.2.2
gamma-GCS
-
Ascaris suum
6.3.2.2
gamma-GCS
-
[Candida] boidinii
6.3.2.2
gamma-GCS
-
Xenopus sp.
6.3.2.2
gamma-GCS
-
Saccharomyces cerevisiae
6.3.2.2
gamma-GCS
-
Escherichia coli
6.3.2.2
gamma-GCS
-
Rattus norvegicus
6.3.2.2
gamma-GCS
-
Trypanosoma brucei
6.3.2.2
gamma-GCS
-
Arabidopsis thaliana
6.3.2.2
gamma-GCS
-
Acidithiobacillus ferrooxidans
6.3.2.2
gamma-GCS
-
Leishmania tarentolae
6.3.2.2
gamma-GCS
-
Mus musculus
6.3.2.2
gamma-GCS
-
Schizosaccharomyces pombe
6.3.2.2
gamma-GCS
-
Homo sapiens
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Sus scrofa
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Bos taurus
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Ovis aries
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Nicotiana tabacum
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Proteus mirabilis
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Ascaris suum
6.3.2.2
gamma-Glutamylcysteine synthetase
-
[Candida] boidinii
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Xenopus sp.
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Saccharomyces cerevisiae
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Escherichia coli
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Rattus norvegicus
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Trypanosoma brucei
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Arabidopsis thaliana
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Acidithiobacillus ferrooxidans
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Leishmania tarentolae
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Mus musculus
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Schizosaccharomyces pombe
6.3.2.2
gamma-Glutamylcysteine synthetase
-
Homo sapiens
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
6.3.2.2
ATP
-
Nicotiana tabacum
6.3.2.2
ATP
-
Proteus mirabilis
6.3.2.2
ATP
-
Ascaris suum
6.3.2.2
ATP
-
[Candida] boidinii
6.3.2.2
ATP
-
Xenopus sp.
6.3.2.2
ATP
-
Saccharomyces cerevisiae
6.3.2.2
ATP
-
Escherichia coli
6.3.2.2
ATP
-
Trypanosoma brucei
6.3.2.2
ATP
-
Arabidopsis thaliana
6.3.2.2
ATP
-
Acidithiobacillus ferrooxidans
6.3.2.2
ATP
-
Leishmania tarentolae
6.3.2.2
ATP
-
Schizosaccharomyces pombe
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Sus scrofa
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Bos taurus
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Ovis aries
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Homo sapiens
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Rattus norvegicus
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Mus musculus
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6.3.2.2
additional information
-
additional information
the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
0.06
-
buthionine sulfone
-
Rattus norvegicus
6.3.2.2
0.11
-
GSH
-
Ascaris suum
6.3.2.2
0.15
-
L-buthionine-R-sulfoximine
-
Rattus norvegicus
6.3.2.2
0.42
-
GSH
-
Nicotiana tabacum
6.3.2.2
1
-
GSH
heavy subunit
Homo sapiens
6.3.2.2
1.1
-
GSH
-
Trypanosoma brucei
6.3.2.2
1.8
-
GSH
heavy subunit
Rattus norvegicus
6.3.2.2
1.8
-
GSH
heavy subunit, the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
2
-
GSH
about, strain B
Escherichia coli
6.3.2.2
2.3
-
GSH
-
Rattus norvegicus
6.3.2.2
2.3
-
GSH
the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
2.5
-
4-methylene-L-glutamate
-
Rattus norvegicus
6.3.2.2
2.7
-
S-sulfo-homocysteine
-
Rattus norvegicus
6.3.2.2
3.1
-
GSH
-
[Candida] boidinii
6.3.2.2
3.3
-
GSH
holoenzyme
Homo sapiens
6.3.2.2
4
-
GSH
about, strain KM
Escherichia coli
6.3.2.2
7.75
-
5-Chloro-4-oxo-L-norvaline
-
Rattus norvegicus
6.3.2.2
8.2
-
GSH
holoenzyme
Rattus norvegicus
6.3.2.2
12.5
-
ophthalmic acid
noncompetitive
Rattus norvegicus
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
6.3.2.2
H2O2
induction of enzyme expression, increase in activity in V79 cells independent on transcription level
Homo sapiens
6.3.2.2
H2O2
induction of in enzyme expression and activity
Saccharomyces cerevisiae
Application (protein specific)
EC Number
Application
Commentary
Organism
6.3.2.2
medicine
enzyme inhibitor L-buthionine-S-sulfoximine is used to modulate GSH levels in cancer patients, overview
Homo sapiens
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.2.2
DNA sequence determination and analysis
[Candida] boidinii
6.3.2.2
DNA sequence determination and analysis
Escherichia coli
6.3.2.2
DNA sequence determination and analysis
Arabidopsis thaliana
6.3.2.2
DNA sequence determination and analysis
Leishmania tarentolae
6.3.2.2
DNA sequence determination and analysis, gene Gsc1, expression in and functional complementation of an enzyme-deficient mutant strain
Schizosaccharomyces pombe
6.3.2.2
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
Saccharomyces cerevisiae
6.3.2.2
DNA sequence determination and analysis, heavy and light subunits, overexpression of catalytic subunit and holoenzyme in Escherichia coli BL21(DE3)
Rattus norvegicus
6.3.2.2
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
Homo sapiens
6.3.2.2
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
Homo sapiens
6.3.2.2
DNA sequence determination and analysis, mapping to chromosome 9, band D-E, heavy and light subunits
Mus musculus
6.3.2.2
DNA sequence determination and analysis, overexpression in Escherichia coli
Trypanosoma brucei
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
6.3.2.2
ATP
-
Nicotiana tabacum
6.3.2.2
ATP
-
Proteus mirabilis
6.3.2.2
ATP
-
Ascaris suum
6.3.2.2
ATP
-
[Candida] boidinii
6.3.2.2
ATP
-
Xenopus sp.
6.3.2.2
ATP
-
Saccharomyces cerevisiae
6.3.2.2
ATP
-
Escherichia coli
6.3.2.2
ATP
-
Trypanosoma brucei
6.3.2.2
ATP
-
Arabidopsis thaliana
6.3.2.2
ATP
-
Acidithiobacillus ferrooxidans
6.3.2.2
ATP
-
Leishmania tarentolae
6.3.2.2
ATP
-
Schizosaccharomyces pombe
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Sus scrofa
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Bos taurus
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Ovis aries
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Homo sapiens
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Rattus norvegicus
6.3.2.2
ATP
the gamma-phosphate is located close to the glutamate binding site by the glycine-rich P-loop, built by the motif M(A/G)FGMGXXCLQ, to facilitate the formation of the enzyme-bound reaction intermediate gamma-glutamyl-phosphate
Mus musculus
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
6.3.2.2
H150A
site-directed mutagenesis, inactive mutant
Rattus norvegicus
6.3.2.2
K38N
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
Rattus norvegicus
6.3.2.2
K38Q
site-directed mutagenesis, 50% reduced activity and 2 to 3fold increased Km for L-Glu compared to the wild-type
Rattus norvegicus
6.3.2.2
K38R
site-directed mutagenesis, slightly decreased activity
Rattus norvegicus
6.3.2.2
additional information
mutation of yAP-1 consensus sequence inhibits binding of yAP-1 protein, rendering the GSH1 promotor nonresponsive to exogenously expressed yAP-1
Saccharomyces cerevisiae
6.3.2.2
additional information
mutational analysis of the 5'-flanking sequence of the heavy subunit, site-directed mutagenesis
Homo sapiens
General Stability (protein specific)
EC Number
General Stability
Organism
6.3.2.2
enzyme is inactivated by freezing
Sus scrofa
6.3.2.2
enzyme is inactivated by freezing
Bos taurus
6.3.2.2
enzyme is inactivated by freezing
Ovis aries
6.3.2.2
enzyme is inactivated by freezing
Proteus mirabilis
6.3.2.2
enzyme is inactivated by freezing
[Candida] boidinii
6.3.2.2
enzyme is inactivated by freezing
Mus musculus
6.3.2.2
enzyme is inactivated by freezing
Homo sapiens
6.3.2.2
enzyme is inactivated by freezing
Rattus norvegicus
6.3.2.2
glycerol is required for enzyme stability during storage
Homo sapiens
6.3.2.2
glycerol is required for enzyme stability during storage
Rattus norvegicus
6.3.2.2
inactivated by freezing
Mus musculus
6.3.2.2
L-glutamate stabilizes the enzyme during purification
Rattus norvegicus
6.3.2.2
L-glutamate stabilizes the enzyme during purification,
Homo sapiens
6.3.2.2
L-glutamate stabilizes the enzyme during purification,
Rattus norvegicus
6.3.2.2
Mn2+ destabilizes the enzyme during purification
Homo sapiens
6.3.2.2
Mn2+ destabilizes the enzyme during purification
Rattus norvegicus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
6.3.2.2
4-methylene-L-glutamate
-
Rattus norvegicus
6.3.2.2
4-methylene-L-glutamate
weak, competitive
Rattus norvegicus
6.3.2.2
5-Chloro-4-oxo-L-norvaline
-
Rattus norvegicus
6.3.2.2
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
Rattus norvegicus
6.3.2.2
buthionine sulfone
-
Rattus norvegicus
6.3.2.2
buthionine sulfoximine
-
Nicotiana tabacum
6.3.2.2
buthionine sulfoximine
-
Ascaris suum
6.3.2.2
buthionine sulfoximine
-
[Candida] boidinii
6.3.2.2
buthionine sulfoximine
-
Saccharomyces cerevisiae
6.3.2.2
buthionine sulfoximine
-
Arabidopsis thaliana
6.3.2.2
buthionine sulfoximine
-
Leishmania tarentolae
6.3.2.2
buthionine sulfoximine
-
Schizosaccharomyces pombe
6.3.2.2
Chloroacetone
-
Rattus norvegicus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Sus scrofa
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Bos taurus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Ovis aries
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Rattus norvegicus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Mus musculus
6.3.2.2
cysteamine
rapid inactivation, reversible by thiols
Homo sapiens
6.3.2.2
D-3-amino-1-chloro-2-pentanone
-
Rattus norvegicus
6.3.2.2
gamma-methylene-D-glutamate
-
Rattus norvegicus
6.3.2.2
GSH
-
Homo sapiens
6.3.2.2
GSH
-
Trypanosoma brucei
6.3.2.2
GSH
feedback inhibition
Sus scrofa
6.3.2.2
GSH
feedback inhibition
Bos taurus
6.3.2.2
GSH
feedback inhibition
Ovis aries
6.3.2.2
GSH
feedback inhibition
Nicotiana tabacum
6.3.2.2
GSH
feedback inhibition
Ascaris suum
6.3.2.2
GSH
feedback inhibition
[Candida] boidinii
6.3.2.2
GSH
feedback inhibition
Escherichia coli
6.3.2.2
GSH
feedback inhibition
Trypanosoma brucei
6.3.2.2
GSH
feedback inhibition
Mus musculus
6.3.2.2
GSH
feedback inhibition
Homo sapiens
6.3.2.2
GSH
feedback inhibition, competitive to L-Glu
Rattus norvegicus
6.3.2.2
iodoacetamide
-
Rattus norvegicus
6.3.2.2
L-buthionine sulfone
competitive, reversible
Rattus norvegicus
6.3.2.2
L-buthionine-R-sulfoximine
-
Escherichia coli
6.3.2.2
L-buthionine-R-sulfoximine
-
Homo sapiens
6.3.2.2
L-buthionine-R-sulfoximine
mechanism-based, competitive, reversible
Rattus norvegicus
6.3.2.2
L-buthionine-S-sulfoximine
strong inhibition
Escherichia coli
6.3.2.2
L-buthionine-S-sulfoximine
strong inhibition
Homo sapiens
6.3.2.2
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
Rattus norvegicus
6.3.2.2
methionine sulfoximine
-
Mus musculus
6.3.2.2
methionine sulfoximine
competitive and reversible
Rattus norvegicus
6.3.2.2
additional information
inhibition mechanisms, no inhibition by L-homocysteine sulfonate
Rattus norvegicus
6.3.2.2
additional information
no inhibition by alpha-ethyl-methionine sulfoximine
Mus musculus
6.3.2.2
additional information
no inhibition by cysteamine or slowly at high concentration
Escherichia coli
6.3.2.2
NO
-
Mus musculus
6.3.2.2
ophthalmic acid
-
Rattus norvegicus
6.3.2.2
S-butyl-DL-homocysteine-SR-sulfoximine
-
Rattus norvegicus
6.3.2.2
S-butyl-DL-homocysteine-SR-sulfoximine
-
Mus musculus
6.3.2.2
S-nitroso-L-cysteine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
Rattus norvegicus
6.3.2.2
S-nitroso-L-cysteinylglycine
inactivation, prevented by pretreatment with ATP and L-SR-buthionine sulfoximine in absence of Mg2+
Rattus norvegicus
6.3.2.2
S-sulfo-homocysteine
-
Rattus norvegicus
6.3.2.2
S-sulfo-L-cysteine
-
Rattus norvegicus
6.3.2.2
Trinitrobenzene sulfonate
inactivates the enzyme
Rattus norvegicus
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6.3.2.2
additional information
-
additional information
the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
0.06
-
buthionine sulfone
-
Rattus norvegicus
6.3.2.2
0.11
-
GSH
-
Ascaris suum
6.3.2.2
0.15
-
L-buthionine-R-sulfoximine
-
Rattus norvegicus
6.3.2.2
0.42
-
GSH
-
Nicotiana tabacum
6.3.2.2
1
-
GSH
heavy subunit
Homo sapiens
6.3.2.2
1.1
-
GSH
-
Trypanosoma brucei
6.3.2.2
1.8
-
GSH
heavy subunit
Rattus norvegicus
6.3.2.2
1.8
-
GSH
heavy subunit, the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
2
-
GSH
about, strain B
Escherichia coli
6.3.2.2
2.3
-
GSH
-
Rattus norvegicus
6.3.2.2
2.3
-
GSH
the Ki for GSH is tissue-dependent
Rattus norvegicus
6.3.2.2
2.5
-
4-methylene-L-glutamate
-
Rattus norvegicus
6.3.2.2
2.7
-
S-sulfo-homocysteine
-
Rattus norvegicus
6.3.2.2
3.1
-
GSH
-
[Candida] boidinii
6.3.2.2
3.3
-
GSH
holoenzyme
Homo sapiens
6.3.2.2
4
-
GSH
about, strain KM
Escherichia coli
6.3.2.2
7.75
-
5-Chloro-4-oxo-L-norvaline
-
Rattus norvegicus
6.3.2.2
8.2
-
GSH
holoenzyme
Rattus norvegicus
6.3.2.2
12.5
-
ophthalmic acid
noncompetitive
Rattus norvegicus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.3.2.2
additional information
-
additional information
kinetics, kinetic mechanism
Rattus norvegicus
6.3.2.2
0.09
-
L-cysteine
strain B
Escherichia coli
6.3.2.2
0.1
-
L-cysteine
strain W
Escherichia coli
6.3.2.2
0.1
-
ATP
strain B
Escherichia coli
6.3.2.2
0.1
-
L-cysteine
holoenzyme
Homo sapiens
6.3.2.2
0.13
-
L-cysteine
heavy subunit
Homo sapiens
6.3.2.2
0.15
-
L-cysteine
-
Proteus mirabilis
6.3.2.2
0.16
-
ATP
-
Proteus mirabilis
6.3.2.2
0.19
-
L-cysteine
-
Nicotiana tabacum
6.3.2.2
0.2
-
ATP
-
[Candida] boidinii
6.3.2.2
0.2
-
L-cysteine
strain KM
Escherichia coli
6.3.2.2
0.2
-
ATP
holoenzyme
Rattus norvegicus
6.3.2.2
0.2
-
L-cysteine
heavy subunit and holoenzyme
Rattus norvegicus
6.3.2.2
0.24
-
L-glutamate
-
Trypanosoma brucei
6.3.2.2
0.31
-
L-alpha-aminobutyrate
-
Ascaris suum
6.3.2.2
0.4
-
L-cysteine
-
[Candida] boidinii
6.3.2.2
0.4
-
ATP
holoenzyme
Homo sapiens
6.3.2.2
0.41
-
L-cysteine
-
Ascaris suum
6.3.2.2
0.5
-
L-glutamate
strain B
Escherichia coli
6.3.2.2
0.69
-
L-cysteine
-
Trypanosoma brucei
6.3.2.2
0.7
-
L-glutamate
strain W
Escherichia coli
6.3.2.2
0.71
-
ATP
-
Trypanosoma brucei
6.3.2.2
0.94
-
L-glutamate
-
Ascaris suum
6.3.2.2
1
-
L-alpha-aminobutyrate
-
Rattus norvegicus
6.3.2.2
1.3
-
L-alpha-aminobutyrate
-
Escherichia coli
6.3.2.2
1.4
-
L-glutamate
-
[Candida] boidinii
6.3.2.2
1.4
-
L-glutamate
holoenzyme
Rattus norvegicus
6.3.2.2
1.41
-
ATP
-
Ascaris suum
6.3.2.2
1.6
-
L-glutamate
-
Proteus mirabilis
6.3.2.2
1.7
-
L-glutamate
strain KM
Escherichia coli
6.3.2.2
1.9
-
L-glutamate
holoenzyme
Homo sapiens
6.3.2.2
2.3
-
L-alpha-aminobutyrate
-
Homo sapiens
6.3.2.2
3.2
-
L-glutamate
heavy subunit
Homo sapiens
6.3.2.2
7.3
-
(R)-beta-amino-iso-butyrate
-
Bos taurus
6.3.2.2
10.4
-
L-glutamate
-
Nicotiana tabacum
6.3.2.2
13.3
-
(S)-beta-amino-iso-butyrate
-
Bos taurus
6.3.2.2
18.2
-
L-glutamate
heavy subunit
Rattus norvegicus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
6.3.2.2
cytosol
exclusively
Sus scrofa
5829
-
6.3.2.2
cytosol
exclusively
Bos taurus
5829
-
6.3.2.2
cytosol
exclusively
Ovis aries
5829
-
6.3.2.2
cytosol
exclusively
Homo sapiens
5829
-
6.3.2.2
cytosol
exclusively
Rattus norvegicus
5829
-
6.3.2.2
cytosol
exclusively
Mus musculus
5829
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.3.2.2
Mg2+
required, bound to the erythrocyte enzyme
Homo sapiens
6.3.2.2
Mg2+
required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by 25%
Rattus norvegicus
6.3.2.2
Mg2+
required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by only 25%
Rattus norvegicus
6.3.2.2
Mn2+
bound to the erythrocyte enzyme
Homo sapiens
6.3.2.2
Mn2+
bound to the kidney enzyme, can substitute for Mg2+ by 25%
Rattus norvegicus
6.3.2.2
Mn2+
bound to the kidney enzyme, can substitute for Mg2+ by only 25%
Rattus norvegicus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
6.3.2.2
30500
-
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
30600
-
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
30700
-
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
31000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
34000
-
2 * 34000
Nicotiana tabacum
6.3.2.2
49300
-
x * 49300, catalytic subunit
Acidithiobacillus ferrooxidans
6.3.2.2
58200
-
1 * 58200
Escherichia coli
6.3.2.2
59900
-
1 * 59900, catalytic unit
Arabidopsis thaliana
6.3.2.2
60000
-
2 * 60000, SDS-PAGE
[Candida] boidinii
6.3.2.2
60000
-
1 * 60000, about
Proteus mirabilis
6.3.2.2
71400
-
x * 71400, catalytic subunit
Schizosaccharomyces pombe
6.3.2.2
72600
-
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
72700
-
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
72800
-
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
73000
-
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
77500
-
1 * 77500, catalytic unit
Trypanosoma brucei
6.3.2.2
78100
-
1 * 78100, catalytic unit
Leishmania tarentolae
6.3.2.2
78300
-
x * 78300, catalytic subunit
Saccharomyces cerevisiae
6.3.2.2
100000
-
kidney enzyme, native PAGE
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
6.3.2.2
ATP + L-Glu + L-Cys
Sus scrofa
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
Bos taurus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Ovis aries
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
Nicotiana tabacum
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
Proteus mirabilis
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
Ascaris suum
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
[Candida] boidinii
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
Xenopus sp.
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
Saccharomyces cerevisiae
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
Escherichia coli
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
Trypanosoma brucei
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
Arabidopsis thaliana
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
Acidithiobacillus ferrooxidans
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
Leishmania tarentolae
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
Schizosaccharomyces pombe
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
Rattus norvegicus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Mus musculus
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
Homo sapiens
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
ADP + phosphate + gamma-L-Glu-L-Cys
-
Homo sapiens
ir
6.3.2.2
additional information
Sus scrofa
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Sus scrofa
?
6.3.2.2
additional information
Bos taurus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Bos taurus
?
6.3.2.2
additional information
Ovis aries
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Ovis aries
?
6.3.2.2
additional information
Mus musculus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
?
-
Mus musculus
?
6.3.2.2
additional information
Homo sapiens
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
?
-
Homo sapiens
?
6.3.2.2
additional information
Rattus norvegicus
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
?
-
Rattus norvegicus
?
6.3.2.2
additional information
Trypanosoma brucei
most of the GSH produced in this pathway is converted to trypanothione
?
-
Trypanosoma brucei
?
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
6.3.2.2
phosphoprotein
the heavy, catalytic subunit can be phosphorylated by dibutyrl cAMP in hepatocytes, and by protein kinase C, protein kinase A, and Ca2+/calmodulin-dpendent kinas II on serine and threonine residues in presence of Mg2+, regulatory role of dephosphorylation/phosphorylation in vivo
Rattus norvegicus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.2.2
-
Proteus mirabilis
6.3.2.2
-
Saccharomyces cerevisiae
6.3.2.2
-
Escherichia coli
6.3.2.2
from erythrocyte
Ovis aries
6.3.2.2
from erythrocyte, from malignant astrocytoma cell line, recombinant from Escherichia coli to homogeneity
Homo sapiens
6.3.2.2
from kidney, liver and erythrocytes, recombinant catalytic subunit and holoenzyme from Escherichia coli to homogeneity
Rattus norvegicus
6.3.2.2
from lens
Bos taurus
6.3.2.2
from liver
Sus scrofa
6.3.2.2
from liver
Xenopus sp.
6.3.2.2
from reproductive tissue
Ascaris suum
6.3.2.2
partially
Nicotiana tabacum
6.3.2.2
recombinant from Escherchia coli to homogeneity
Trypanosoma brucei
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
6.3.2.2
astrocytoma cell
malignant cell line
Homo sapiens
-
6.3.2.2
brain
-
Homo sapiens
-
6.3.2.2
brain
-
Rattus norvegicus
-
6.3.2.2
colon
-
Homo sapiens
-
6.3.2.2
erythrocyte
-
Ovis aries
-
6.3.2.2
erythrocyte
-
Homo sapiens
-
6.3.2.2
erythrocyte
-
Rattus norvegicus
-
6.3.2.2
heart
-
Homo sapiens
-
6.3.2.2
kidney
-
Sus scrofa
-
6.3.2.2
kidney
-
Bos taurus
-
6.3.2.2
kidney
-
Ovis aries
-
6.3.2.2
kidney
-
Homo sapiens
-
6.3.2.2
kidney
-
Rattus norvegicus
-
6.3.2.2
kidney
-
Mus musculus
-
6.3.2.2
lens
-
Bos taurus
-
6.3.2.2
liver
-
Sus scrofa
-
6.3.2.2
liver
-
Bos taurus
-
6.3.2.2
liver
-
Ovis aries
-
6.3.2.2
liver
-
Xenopus sp.
-
6.3.2.2
liver
-
Homo sapiens
-
6.3.2.2
liver
-
Rattus norvegicus
-
6.3.2.2
liver
-
Mus musculus
-
6.3.2.2
lung
-
Homo sapiens
-
6.3.2.2
macrophage
-
Mus musculus
-
6.3.2.2
additional information
expression patterns of both subunits in the tissues, overview, 2 transcript different in size for both the heavy and light subunit occur in the tissues, some tumors overexpress only the heavy subunit rather than the holoenzyme
Homo sapiens
-
6.3.2.2
additional information
expression patterns of both subunits in the tissues, overview, 2 transcripts different in size for both the heavy and light subunit occur in the tissues, some tumors overexpress only the heavy subunit rather than the holoenzyme
Homo sapiens
-
6.3.2.2
ovary
-
Homo sapiens
-
6.3.2.2
pancreas
-
Homo sapiens
-
6.3.2.2
peripheral blood
-
Homo sapiens
-
6.3.2.2
placenta
-
Homo sapiens
-
6.3.2.2
prostate
-
Homo sapiens
-
6.3.2.2
reproductive system
-
Ascaris suum
-
6.3.2.2
skeletal muscle
-
Homo sapiens
-
6.3.2.2
small intestine
-
Homo sapiens
-
6.3.2.2
spleen
-
Homo sapiens
-
6.3.2.2
testis
-
Homo sapiens
-
6.3.2.2
thymus
-
Homo sapiens
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
6.3.2.2
additional information
-
-
Rattus norvegicus
6.3.2.2
0.001
-
native COS cells
Homo sapiens
6.3.2.2
0.013
-
-
[Candida] boidinii
6.3.2.2
0.014
-
transformed COS cells expressing both the recombinant subunits at equal amounts
Homo sapiens
6.3.2.2
0.038
-
transformed COS cells expressing the recombinant catalytic subunit
Homo sapiens
6.3.2.2
25
-
purified enzyme
Rattus norvegicus
6.3.2.2
25
-
purified recombinant enzyme
Homo sapiens
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Sus scrofa
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Bos taurus
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Ovis aries
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Homo sapiens
6.3.2.2
-20°C, purified enzyme, 25% glycerol, indefinitely stable
Rattus norvegicus
6.3.2.2
-80°C, enzyme is very stable at
Escherichia coli
6.3.2.2
-80°C, enzyme is very stable at
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
6.3.2.2
ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + beta-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + beta-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + beta-methyl-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + beta-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + D-Glu + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-alpha-aminomethylglutarate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-alpha-aminomethylglutaryl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-alpha-aminomethylsuccinate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-alpha-aminomethylsuccinyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + DL-beta-aminoadipate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + DL-beta-aminoadipyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu
-
649263
Rattus norvegicus
ADP + phosphate + 5-oxoproline
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + (R)-beta-amino-iso-butyrate
2fold less reactive as the S-isomer
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-(R)-beta-amino-iso-butyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + (S)-beta-amino-iso-butyrate
2fold as reactive as the R-isomer
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-(S)-beta-amino-iso-butyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + beta-chloro-L-alanine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + DL-allylglycine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + DL-beta-amino-iso-butyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + Gly
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-Gly
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-2-aminobutanoate
-
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
-
-
?
6.3.2.2
ATP + L-Glu + L-alanine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alanine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminobutyrate
-
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-alpha-aminoheptanoate
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-alpha-aminoheptanoate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Sus scrofa
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Ovis aries
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Nicotiana tabacum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Proteus mirabilis
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
[Candida] boidinii
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Xenopus sp.
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Saccharomyces cerevisiae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Trypanosoma brucei
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Arabidopsis thaliana
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Acidithiobacillus ferrooxidans
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Leishmania tarentolae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Mus musculus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Schizosaccharomyces pombe
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
-
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Sus scrofa
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Sus scrofa
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Ovis aries
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ovis aries
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Nicotiana tabacum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Nicotiana tabacum
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Proteus mirabilis
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Proteus mirabilis
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Ascaris suum
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Ascaris suum
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
[Candida] boidinii
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
[Candida] boidinii
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Xenopus sp.
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Xenopus sp.
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Saccharomyces cerevisiae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Saccharomyces cerevisiae
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Escherichia coli
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Escherichia coli
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Trypanosoma brucei
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Trypanosoma brucei
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Arabidopsis thaliana
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Arabidopsis thaliana
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Acidithiobacillus ferrooxidans
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Acidithiobacillus ferrooxidans
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Leishmania tarentolae
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Leishmania tarentolae
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Schizosaccharomyces pombe
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Schizosaccharomyces pombe
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Mus musculus
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Mus musculus
ir
6.3.2.2
ATP + L-Glu + L-Cys
rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview
649263
Homo sapiens
ADP + phosphate + gamma-L-Glu-L-Cys
-
649263
Homo sapiens
ir
6.3.2.2
ATP + L-Glu + L-homocysteine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-homocysteine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-homoserine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-homoserine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-norleucine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-norleucine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-norvaline
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-norvaline
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-serine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-serine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-threonine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-L-threonine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + L-Glu + L-threonine
allo-L-threonine is a 5fold better substrate than L-threonine
649263
Bos taurus
ADP + phosphate + gamma-L-Glu-L-threonine
-
649263
Bos taurus
ir
6.3.2.2
ATP + L-Glu + S-methyl-L-cysteine
-
649263
Rattus norvegicus
ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + threo-beta-hydroxy-DL-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + threo-beta-hydroxy-DL-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
ATP + threo-gamma-hydroxy-L-glutamate + L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ADP + phosphate + threo-gamma-hydroxy-L-glutamyl-L-alpha-aminobutyrate
-
649263
Rattus norvegicus
ir
6.3.2.2
additional information
substrate specificity
649263
Escherichia coli
?
-
649263
Escherichia coli
?
6.3.2.2
additional information
substrate specificity
649263
Homo sapiens
?
-
649263
Homo sapiens
?
6.3.2.2
additional information
substrate specificity, beta-alanine, (R,S)-beta-amino-n-butyrate, and (R,S)-alpha-ethyl-beta-alanine are no substrates
649263
Bos taurus
?
-
649263
Bos taurus
?
6.3.2.2
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
649263
Rattus norvegicus
?
-
649263
Rattus norvegicus
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Sus scrofa
?
-
649263
Sus scrofa
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Bos taurus
?
-
649263
Bos taurus
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Ovis aries
?
-
649263
Ovis aries
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH
649263
Mus musculus
?
-
649263
Mus musculus
?
6.3.2.2
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
649263
Homo sapiens
?
-
649263
Homo sapiens
?
6.3.2.2
additional information
GSH synthesis is controlled by the amount of enzyme, L-cysteine and by feedback inhibition exerted by GSH, regulation by dephosphorylation/phosphorylation
649263
Rattus norvegicus
?
-
649263
Rattus norvegicus
?
6.3.2.2
additional information
most of the GSH produced in this pathway is converted to trypanothione
649263
Trypanosoma brucei
?
-
649263
Trypanosoma brucei
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
6.3.2.2
?
x * 49300, catalytic subunit
Acidithiobacillus ferrooxidans
6.3.2.2
?
x * 71400, catalytic subunit
Schizosaccharomyces pombe
6.3.2.2
?
x * 78300, catalytic subunit
Saccharomyces cerevisiae
6.3.2.2
dimer
2 * 60000, SDS-PAGE
[Candida] boidinii
6.3.2.2
dimer
2 * 34000
Nicotiana tabacum
6.3.2.2
dimer
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
Rattus norvegicus
6.3.2.2
dimer
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
Mus musculus
6.3.2.2
dimer
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
Homo sapiens
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Sus scrofa
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Bos taurus
6.3.2.2
dimer
1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
Ovis aries
6.3.2.2
monomer
1 * 58200
Escherichia coli
6.3.2.2
monomer
1 * 59900, catalytic unit
Arabidopsis thaliana
6.3.2.2
monomer
1 * 60000, about
Proteus mirabilis
6.3.2.2
monomer
1 * 77500, catalytic unit
Trypanosoma brucei
6.3.2.2
monomer
1 * 78100, catalytic unit
Leishmania tarentolae
6.3.2.2
More
quarternary structure
Ovis aries
6.3.2.2
More
quarternary structure
Mus musculus
6.3.2.2
More
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
Rattus norvegicus
6.3.2.2
More
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
Homo sapiens
6.3.2.2
More
quaternary structure
Sus scrofa
6.3.2.2
More
quaternary structure
Bos taurus
6.3.2.2
More
quaternary structure
Mus musculus
6.3.2.2
More
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
Trypanosoma brucei
6.3.2.2
More
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
Leishmania tarentolae