EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.18 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL1-Blue | Mus musculus |
2.5.1.18 | expression of His-tagged wild-type enzyme in Escherichia coli strain XL1-Blue | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.18 | R234W | site-directed mutagenesis | Mus musculus |
2.5.1.18 | W234R | site-directed mutagenesis | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.18 | additional information | - |
additional information | kinetic analysis, overview | Rattus norvegicus | |
2.5.1.18 | additional information | - |
additional information | kinetic analysis of wild-type and mutant enzymes, overview | Mus musculus | |
2.5.1.18 | additional information | - |
additional information | kinetic analysis of wild-type and mutant enzymes, overview | Homo sapiens | |
2.5.1.18 | 0.05 | - |
iodohexane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 0.058 | - |
iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 0.059 | - |
1-iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 0.083 | - |
iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 0.085 | - |
iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 0.36 | - |
iodobutane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 0.56 | - |
1-Iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 0.91 | - |
1-iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 1.89 | - |
iodomethane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.18 | Homo sapiens | P30711 | - |
- |
2.5.1.18 | Mus musculus | - |
- |
- |
2.5.1.18 | Rattus norvegicus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.18 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain XL1-Blue by nickel affinity chromatography | Mus musculus |
2.5.1.18 | recombinant His-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by nickel affinity chromatography | Rattus norvegicus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.5.1.18 | additional information | - |
substrate specificities of recombinant His-tagged wild-type and mutant enzymes, overview | Mus musculus |
2.5.1.18 | additional information | - |
substrate specificities of recombinant His-tagged wild-type and mutant enzymes, overview | Homo sapiens |
2.5.1.18 | additional information | - |
substrate specificity of recombinant His-tagged enzyme, overview | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.18 | 1,2-epoxy-3-(4-nitrophenoxy)-propane + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | 1,2-epoxy-3-(4-nitrophenoxy)-propane + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | 1,2-epoxy-3-(4-nitrophenoxy)-propane + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | 4-nitrobenzyl chloride + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | 4-nitrobenzyl chloride + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | 4-nitrobenzyl chloride + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | 4-nitrophenethyl bromide + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | 4-nitrophenethyl bromide + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | 4-nitrophenethyl bromide + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | allyl isothiocyanate + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | allyl isothiocyanate + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | allyl isothiocyanate + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | benzyl isothiocyanate + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | benzyl isothiocyanate + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | benzyl isothiocyanate + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | cumene hydroperoxide + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | cumene hydroperoxide + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | cumene hydroperoxide + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | glutathione + 1-chloro-2,4-dinitrobenzene | - |
Mus musculus | S-(2,4-dinitrophenyl)glutathione + HCl | - |
? | |
2.5.1.18 | glutathione + 1-chloro-2,4-dinitrobenzene | - |
Rattus norvegicus | S-(2,4-dinitrophenyl)glutathione + HCl | - |
? | |
2.5.1.18 | glutathione + 1-chloro-2,4-dinitrobenzene | - |
Homo sapiens | S-(2,4-dinitrophenyl)glutathione + HCl | - |
? | |
2.5.1.18 | glutathione + 1-iodobutane | - |
Mus musculus | iodide + butyl-glutathione | - |
? | |
2.5.1.18 | glutathione + 1-iodohexane | - |
Mus musculus | iodide + hexyl-glutathione | - |
? | |
2.5.1.18 | glutathione + 1-iodomethane | - |
Mus musculus | iodide + methylglutathione | - |
? | |
2.5.1.18 | hydrogen peroxide + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | hydrogen peroxide + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | hydrogen peroxide + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | iodobutane + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | iodohexane + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | iodomethane + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | additional information | substrate specificity, overview. A major structural determinant of substrate recognition is the H-site, which binds the electrophile in proximity to the nucleophilic sulfur of the second substrate glutathione. H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1 | Mus musculus | ? | - |
? | |
2.5.1.18 | additional information | substrate specificity, overview. A major structural determinant of substrate recognition is the H-site, which binds the electrophile in proximity to the nucleophilic sulfur of the second substrate glutathione. H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1 | Rattus norvegicus | ? | - |
? | |
2.5.1.18 | additional information | substrate specificity, overview. A major structural determinant of substrate recognition is the H-site, which binds the electrophile in proximity to the nucleophilic sulfur of the second substrate glutathione. H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1 | Homo sapiens | ? | - |
? | |
2.5.1.18 | phenethyl isothiocyanate + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | phenethyl isothiocyanate + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | phenethyl isothiocyanate + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | propyl isothiocyanate + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | propyl isothiocyanate + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | propyl isothiocyanate + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | styrene oxide + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | styrene oxide + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | styrene oxide + glutathione | - |
Homo sapiens | ? | - |
? | |
2.5.1.18 | tertiary butyl hydroperoxide + glutathione | - |
Mus musculus | ? | - |
? | |
2.5.1.18 | tertiary butyl hydroperoxide + glutathione | - |
Rattus norvegicus | ? | - |
? | |
2.5.1.18 | tertiary butyl hydroperoxide + glutathione | - |
Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.18 | More | the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview | Mus musculus |
2.5.1.18 | More | the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview | Rattus norvegicus |
2.5.1.18 | More | the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.18 | GST T1-1 | - |
Mus musculus |
2.5.1.18 | GST T1-1 | - |
Rattus norvegicus |
2.5.1.18 | GST T1-1 | - |
Homo sapiens |
2.5.1.18 | theta class glutathione transferase T1-1 | - |
Mus musculus |
2.5.1.18 | theta class glutathione transferase T1-1 | - |
Rattus norvegicus |
2.5.1.18 | theta class glutathione transferase T1-1 | - |
Homo sapiens |
2.5.1.18 | theta class GST | - |
Mus musculus |
2.5.1.18 | theta class GST | - |
Rattus norvegicus |
2.5.1.18 | theta class GST | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.18 | 30 | - |
assay at | Mus musculus |
2.5.1.18 | 30 | - |
assay at | Rattus norvegicus |
2.5.1.18 | 30 | - |
assay at | Homo sapiens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.18 | 0.037 | - |
iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 0.068 | - |
iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 0.137 | - |
1-Iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 0.215 | - |
iodobutane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 3.17 | - |
1-iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 3.52 | - |
iodohexane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 9.16 | - |
iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 238 | - |
1-iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 349 | - |
iodomethane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.18 | 6.5 | 8 | assay at, dependent on the substrate | Mus musculus |
2.5.1.18 | 6.5 | 8 | assay at, dependent on the substrate | Rattus norvegicus |
2.5.1.18 | 6.5 | 8 | assay at, dependent on the substrate | Homo sapiens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.18 | 0.244 | - |
iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 0.59 | - |
iodobutane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 0.701 | - |
iodobutane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 1.17 | - |
iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 54.1 | - |
iodohexane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus | |
2.5.1.18 | 69.8 | - |
iodohexane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 107 | - |
iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Homo sapiens | |
2.5.1.18 | 185 | - |
iodomethane | pH 8.0, 30°C, recombinant enzyme | Rattus norvegicus | |
2.5.1.18 | 263 | - |
iodomethane | pH 8.0, 30°C, recombinant wild-type enzyme | Mus musculus |