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Literature summary for 2.5.1.18 extracted from

  • Skopelitou, K.; Dhavala, P.; Papageorgiou, A.C.; Labrou, N.E.
    A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily (2012), PLoS ONE, 7, e34263.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.18

Cloned(Commentary)

Cloned (Comment) Organism
gene Atu3701, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of His-tagged wild-type and mutant AtuGSTH1-1s in Escherichia coli strain BL21 (DE3) Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
AtuGSTH1-1 in complex with inhibitor S-(4-nitrobenzyl)-glutathione, hanging drop vapor diffusion method, mixing of 0.002 ml of 4.85 mg/ml protein in 15 mM Tris-HCl, pH 7.0, and 10 mM S-(4-nitrobenzyl)-glutathione, with 0.002 ml of well solution 1.4 M Na/K phosphate, pH 8.3, equilibration against 0.8 ml well solution, 16°C, X-ray diffraction structure determination and analysis at 1.4 A resolution Agrobacterium tumefaciens

Protein Variants

Protein Variants Comment Organism
F22A site-directed mutagenesis, the mutant shows reduced glutathione transferase activity and increased glutatione peroxidase activity compared to the wild-type GSTH1-1 Agrobacterium tumefaciens
R187A site-directed mutagenesis, the mutant shows reduced glutathione transferase activity and reduced glutatione peroxidase activity compared to the wild-type GSTH1-1 Agrobacterium tumefaciens
R34A site-directed mutagenesis, almost inactive mutant Agrobacterium tumefaciens
S25A site-directed mutagenesis, the mutant shows reduced glutathione transferase activity and increased glutatione peroxidase activity compared to the wild-type GSTH1-1 Agrobacterium tumefaciens

Inhibitors

Inhibitors Comment Organism Structure
S-(p-nitrobenzyl)-glutathione
-
 Agrobacterium tumefaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state Michaelis-Menten kinetic analysis of AtuGSTH1-1 Agrobacterium tumefaciens
0.085
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant F22A, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens
0.14
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant S25A, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens
0.3
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens
0.34
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant R187A, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens
1.5
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
1.7
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 2-hydroxyethyl disulfide Agrobacterium tumefaciens
1.9
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant S25A Agrobacterium tumefaciens
3.2
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant F22A Agrobacterium tumefaciens
4.1
-
 2-hydroxyethyl disulfide pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
7.1
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant R187A Agrobacterium tumefaciens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Agrobacterium tumefaciens 5829
-

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
-
 gene Atu3701 encoding an eta class GST, i.e. AtuGSTH1-1
-
Agrobacterium tumefaciens C58 / ATCC 33970
-
 gene Atu3701 encoding an eta class GST, i.e. AtuGSTH1-1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant AtuGSTH1-1s from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Agrobacterium tumefaciens

Reaction

Reaction Comment Organism Reaction ID
RX + glutathione = HX + R-S-glutathione catalytic mechanism of isozyme GSTH1-1 Agrobacterium tumefaciens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-chloro-2,4-dinitrobenzene + glutathione
-
 Agrobacterium tumefaciens S-(2,4-dinitrophenyl)glutathione + HCl
-
 ?
1-chloro-2,4-dinitrobenzene + glutathione
-
 Agrobacterium tumefaciens C58 / ATCC 33970 S-(2,4-dinitrophenyl)glutathione + HCl
-
 ?
2-hydroxyethyl disulfide + glutathione
-
 Agrobacterium tumefaciens ?
-
 ?
2-hydroxyethyl disulfide + glutathione
-
 Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
 ?
additional information AtuGSTH1-1 exhibits significant transferase activity against the common substrates aryl halides, as well as very high peroxidase activity towards organic hydroperoxides Agrobacterium tumefaciens ?
-
 ?
additional information AtuGSTH1-1 exhibits significant transferase activity against the common substrates aryl halides, as well as very high peroxidase activity towards organic hydroperoxides Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
 ?

Synonyms

Synonyms Comment Organism
AtuGSTH1-1
-
 Agrobacterium tumefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Agrobacterium tumefaciens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.04
-
 2-hydroxyethyl disulfide pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
0.04
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 2-hydroxyethyl disulfide Agrobacterium tumefaciens
0.53
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
0.53
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Agrobacterium tumefaciens

General Information

General Information Comment Organism
additional information AtuGSTH1-1 lacks the classic catalytic essential residues (Tyr, Ser, Cys) and has instead of the classic catalytic residues, an Arg residue (Arg34), an electron-sharing network, and a bridge of a network of water molecules may form the basis of the catalytic mechanism, Phe22, Ser25, and Arg187 are additional important residues for the enzyme's catalytic efficiency and specificity, overview. GSH binding site, G-site, and electrophilic binding site, H-site, structures, overview. In contrast to other GSTs where the H-site involves C-terminal domain residues, interactions in AtuGSTH1-1 are mainly provided by Arg187 and the long turn between strand b1 andhelix H1, residues 25-33 Agrobacterium tumefaciens
physiological function AtuGSTH1-1 may play an important regulatory role in stress defence mechanism Agrobacterium tumefaciens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.01
-
 2-hydroxyethyl disulfide pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
0.01
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 2-hydroxyethyl disulfide Agrobacterium tumefaciens
0.36
-
 1-chloro-2,4-dinitrobenzene pH 6.5, 37°C, recombinant AtuGSTH1-1 Agrobacterium tumefaciens
0.36
-
 glutathione pH 6.5, 37°C, recombinant AtuGSTH1-1, with 1-chloro-2,4-dinitrobenzene Agrobacterium tumefaciens