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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 | - |
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 |
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 |
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 | ? | - |
? |
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 | - |
- |
- |
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 |
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 |
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 |
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 | - |
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 |
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 |
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 | ? | - |
? |
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 |
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 |
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 |
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 |