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Literature summary extracted from

  • Federici, L.; Masulli, M.; Di Ilio, C.; Allocati, N.
    Characterization of the hydrophobic substrate-binding site of the bacterial beta class glutathione transferase from Proteus mirabilis (2010), Protein Eng. Des. Sel., 23, 743-750.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.18 expression of wild-type and mutant enzymes in Escherichia coli strain XL1-Blue Proteus mirabilis

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.18 F113A site-directed mutagenesis of the H-site residue, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Proteus mirabilis
2.5.1.18 G8A site-directed mutagenesis of the H-site residue Proteus mirabilis
2.5.1.18 H167A site-directed mutagenesis of the H-site residue, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Proteus mirabilis
2.5.1.18 additional information mutations at the H-site can be used to modulate activity at the level of the different catalytic mechanisms operating on the chosen substrates, each mutation showing a different fingerprint, overview Proteus mirabilis
2.5.1.18 S110A site-directed mutagenesis of the H-site residue, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Proteus mirabilis
2.5.1.18 W164A site-directed mutagenesis of the H-site residue the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Proteus mirabilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.18 0.453
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 0.557
-
 glutathione pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 0.577
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 0.599
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 0.651
-
 glutathione pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 0.653
-
 glutathione pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 0.69
-
 glutathione pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 0.696
-
 glutathione pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 0.732
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 0.76
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 1.262
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 1.298
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 1.393
-
 glutathione pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 1.502
-
 glutathione pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 1.863
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 1.95
-
 glutathione pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 2.155
-
 glutathione pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 2.432
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 3.607
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 5.509
-
 glutathione pH 6.5, 25°C, mutant F113A Proteus mirabilis

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.18 Proteus mirabilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.18 recombinant wild-type and mutant enzymes from Escherichia coli strain XL1-Blue by anion exchange chromatography, dialysis, ultrafiltration, and chromatofocussing Proteus mirabilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.18 0.001
-
 purified recombinant mutant W164A, pH 6.5, 25°C, substrate 4-nitrobenzyl chloride Proteus mirabilis
2.5.1.18 0.001
-
 purified recombinant wild-type enzyme, pH 6.5, 25°C, substrate 4-nitrobenzyl chloride Proteus mirabilis
2.5.1.18 0.002
-
 purified recombinant mutant H167A, pH 6.5, 25°C, substrate 4-nitrobenzyl chloride Proteus mirabilis
2.5.1.18 0.004
-
 purified recombinant mutant S110a, pH 6.5, 25°C, substrate 4-nitrobenzyl chloride Proteus mirabilis
2.5.1.18 0.005
-
 purified recombinant mutant F113A, pH 6.5, 25°C, substrate 4-nitrobenzyl chloride Proteus mirabilis
2.5.1.18 0.011
-
 purified recombinant mutant F113A, pH 6.5, 25°C, substrate ethacrynic acid Proteus mirabilis
2.5.1.18 0.017
-
 purified recombinant mutant H167A, pH 6.5, 25°C, substrate ethacrynic acid Proteus mirabilis
2.5.1.18 0.035
-
 purified recombinant mutant S110a, pH 6.5, 25°C, substrate ethacrynic acid Proteus mirabilis
2.5.1.18 0.081
-
 purified recombinant wild-type enzyme, pH 6.5, 25°C, substrate ethacrynic acid Proteus mirabilis
2.5.1.18 0.088
-
 purified recombinant mutant W164A, pH 6.5, 25°C, substrate ethacrynic acid Proteus mirabilis
2.5.1.18 0.17
-
 purified recombinant mutant F113A, pH 6.5, 25°C, substrate 1-chloro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 0.48
-
 purified recombinant mutant H167A, pH 6.5, 25°C, substrate 1-chloro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 0.67
-
 purified recombinant mutant F113A, pH 6.5, 25°C, substrate 1-fluoro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 1.08
-
 purified recombinant wild-type enzyme, pH 6.5, 25°C, substrate 1-chloro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 1.31
-
 purified recombinant mutant S110a, pH 6.5, 25°C, substrate 1-chloro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 1.91
-
 purified recombinant mutant H167A, pH 6.5, 25°C, substrate 1-fluoro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 3.31
-
 purified recombinant mutant S110a, pH 6.5, 25°C, substrate 1-fluoro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 3.69
-
 purified recombinant wild-type enzyme, pH 6.5, 25°C, substrate 1-fluoro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 7.89
-
 purified recombinant mutant W164A, pH 6.5, 25°C, substrate 1-fluoro-2,4-dinitrobenzene Proteus mirabilis
2.5.1.18 22.69
-
 purified recombinant mutant W164A, pH 6.5, 25°C, substrate 1-chloro-2,4-dinitrobenzene Proteus mirabilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.18 1-chloro-2,4-dinitrobenzene + glutathione 1-chloro-2,4-dinitrobenzene is conjugated through a classic SNAr reaction that proceeds in two steps with the formation of an intermediate Meisenheimer complex Proteus mirabilis S-(2,4-dinitrophenyl)glutathione + HCl
-
 ?
2.5.1.18 1-fluoro-2,4-dinitrobenzene + glutathione 1-fluoro-2,4-dinitrobenzene is conjugated through a classic SNAr reaction that proceeds in two steps with the formation of an intermediate Meisenheimer complex Proteus mirabilis S-(2,4-dinitrophenyl)glutathione + HF
-
 ?
2.5.1.18 4-nitrobenzyl chloride + glutathione 4-nitrobenzyl chloride is conjugated through a single-step bimolecular nucleophilic substitution (SN2) with a pentacoordinate intermediate Proteus mirabilis S-(4-nitrobenzyl)glutathione + HCl
-
 ?
2.5.1.18 ethacrynic acid + glutathione ethacrynic acid is conjugated via a Michael addition reaction through the formation of an enole intermediate Proteus mirabilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.18 GSH transferase
-
 Proteus mirabilis
2.5.1.18 PmGST
-
 Proteus mirabilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.18 45
-
 mutant F113A Proteus mirabilis
2.5.1.18 50
-
 wild-type GST, and mutants S110A and W164A Proteus mirabilis
2.5.1.18 60
-
 mutant H167A Proteus mirabilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.18 0.12
-
 glutathione pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 0.2
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 0.43
-
 glutathione pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 0.88
-
 glutathione pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 1.03
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 1.56
-
 glutathione pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 2.13
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 2.59
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 3.18
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 4.37
-
 glutathione pH 6.5, 25°C, mutant H167A Proteus mirabilis
2.5.1.18 4.7
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 6.38
-
 glutathione pH 6.5, 25°C, mutant F113A Proteus mirabilis
2.5.1.18 6.44
-
 glutathione pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 6.78
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 8.66
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant S110A Proteus mirabilis
2.5.1.18 12.2
-
 1-Fluoro-2,4-dinitrobenzene pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 12.4
-
 glutathione pH 6.5, 25°C, wild-type enzyme Proteus mirabilis
2.5.1.18 14.99
-
 glutathione pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 21.44
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 25°C, mutant W164A Proteus mirabilis
2.5.1.18 29.7
-
 glutathione pH 6.5, 25°C, mutant W164A Proteus mirabilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.18 6.5
-
 assay at Proteus mirabilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.18 5 9 activity range, profiles of wild-type and mutant enzymes, overview Proteus mirabilis

General Information

EC Number General Information Comment Organism
2.5.1.18 additional information contribution of different residues in the GSH-binding site to GSH activation, structure analysis of wild-type and mutant enzymes by circular dichroism and fluorospectroscopic analysis, overview Proteus mirabilis