Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Griffith, O.W.; Mulcahy, R.T.
    The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase (1999), Adv. Enzymol. Relat. Areas Mol. Biol., 73, 209-267.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment 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 Comment 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 (Comment) 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

Protein Variants

EC Number Protein Variants Comment 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 Comment 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 Comment 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
6.3.2.2 additional information Trypanosoma brucei most of the GSH produced in this pathway is converted to trypanothione ?
-
?

Organism

EC Number Organism UniProt Comment 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 Comment 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 (Comment) 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 Comment 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 Comment 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + alpha-methyl-DL-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + alpha-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + beta-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + beta-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + beta-methyl-DL-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + beta-methyl-DL-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + D-Glu + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + DL-alpha-aminomethylglutarate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + DL-alpha-aminomethylglutaryl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + DL-alpha-aminomethylsuccinate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + DL-alpha-aminomethylsuccinyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + DL-beta-aminoadipate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + DL-beta-aminoadipyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + L-Glu
-
Rattus norvegicus ADP + phosphate + 5-oxoproline
-
ir
6.3.2.2 ATP + L-Glu + (R)-beta-amino-iso-butyrate 2fold less reactive as the S-isomer Bos taurus ADP + phosphate + gamma-L-Glu-(R)-beta-amino-iso-butyrate
-
ir
6.3.2.2 ATP + L-Glu + (S)-beta-amino-iso-butyrate 2fold as reactive as the R-isomer Bos taurus ADP + phosphate + gamma-L-Glu-(S)-beta-amino-iso-butyrate
-
ir
6.3.2.2 ATP + L-Glu + beta-chloro-L-alanine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine
-
ir
6.3.2.2 ATP + L-Glu + DL-allylglycine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-DL-allylglycine
-
ir
6.3.2.2 ATP + L-Glu + DL-beta-amino-iso-butyrate
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-DL-beta-amino-iso-butyrate
-
ir
6.3.2.2 ATP + L-Glu + Gly
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-Gly
-
ir
6.3.2.2 ATP + L-Glu + L-2-aminobutanoate
-
Escherichia coli ADP + phosphate + gamma-L-Glu-2-aminobutanoate
-
?
6.3.2.2 ATP + L-Glu + L-alanine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-alanine
-
ir
6.3.2.2 ATP + L-Glu + L-alpha-aminobutyrate
-
Bos taurus ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + L-Glu + L-alpha-aminobutyrate
-
Ascaris suum ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + L-Glu + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + L-Glu + L-alpha-aminobutyrate
-
Homo sapiens ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + L-Glu + L-alpha-aminoheptanoate
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-alpha-aminoheptanoate
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Sus scrofa ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Bos taurus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Ovis aries ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Nicotiana tabacum ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Proteus mirabilis ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Ascaris suum ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
[Candida] boidinii ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Xenopus sp. ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Saccharomyces cerevisiae ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Escherichia coli ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Trypanosoma brucei ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Arabidopsis thaliana ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Acidithiobacillus ferrooxidans ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Leishmania tarentolae ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Mus musculus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Schizosaccharomyces pombe ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys
-
Homo sapiens ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Sus scrofa ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Bos taurus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Ovis aries ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Nicotiana tabacum ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Proteus mirabilis ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Ascaris suum ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview [Candida] boidinii ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Xenopus sp. ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Saccharomyces cerevisiae ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Escherichia coli ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Trypanosoma brucei ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Arabidopsis thaliana ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Acidithiobacillus ferrooxidans ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Leishmania tarentolae ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Schizosaccharomyces pombe ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Mus musculus ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-Cys rate limiting and first step in glutathione biosynthesis, GSH metabolism, overview Homo sapiens ADP + phosphate + gamma-L-Glu-L-Cys
-
ir
6.3.2.2 ATP + L-Glu + L-homocysteine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-homocysteine
-
ir
6.3.2.2 ATP + L-Glu + L-homoserine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-homoserine
-
ir
6.3.2.2 ATP + L-Glu + L-norleucine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-norleucine
-
ir
6.3.2.2 ATP + L-Glu + L-norvaline
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-norvaline
-
ir
6.3.2.2 ATP + L-Glu + L-serine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-serine
-
ir
6.3.2.2 ATP + L-Glu + L-threonine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-threonine
-
ir
6.3.2.2 ATP + L-Glu + L-threonine allo-L-threonine is a 5fold better substrate than L-threonine Bos taurus ADP + phosphate + gamma-L-Glu-L-threonine
-
ir
6.3.2.2 ATP + L-Glu + S-methyl-L-cysteine
-
Rattus norvegicus ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine
-
ir
6.3.2.2 ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + threo-beta-hydroxy-DL-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + threo-beta-hydroxy-DL-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 ATP + threo-gamma-hydroxy-L-glutamate + L-alpha-aminobutyrate
-
Rattus norvegicus ADP + phosphate + threo-gamma-hydroxy-L-glutamyl-L-alpha-aminobutyrate
-
ir
6.3.2.2 additional information substrate specificity Escherichia coli ?
-
?
6.3.2.2 additional information substrate specificity 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 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 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 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 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 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 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 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 Rattus norvegicus ?
-
?
6.3.2.2 additional information most of the GSH produced in this pathway is converted to trypanothione Trypanosoma brucei ?
-
?

Subunits

EC Number Subunits Comment 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 Comment 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 Comment 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 Comment 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