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EC Tree
IUBMB Comments A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
The taxonomic range for the selected organisms is: Sus scrofa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3,
more
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alpha-class glutathione transferase
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glutathione transferase A1-1
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glutathione S-alkyl transferase
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glutathione S-aralkyltransferase
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glutathione S-aryltransferase
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glutathione S-transferase
glutathione S-transferase X
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GSH S-transferase
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S-(hydroxyalkyl)glutathione lyase
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glutathione S-transferase
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glutathione S-transferase
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glutathione S-transferase
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aryl group transfer
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RX:glutathione R-transferase
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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?
5-androstene-3,17-dione + glutathione
?
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?
5-pregnene-3,20-dione + glutathione
?
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?
phenethyl isothiocyanate + glutathione
?
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?
trans-2-nonenal + glutathione
?
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?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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?
glutathione + 1,2-dinitrobenzene
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?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
glutathione + 2,5-dinitrophenol
?
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glutathione + 3,4-dinitrobenzoic acid
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?
glutathione + 4-nitrobenzyl chloride
?
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?
glutathione + 5-nitrofurfural
?
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glutathione + 5-nitrofurfural diacetal
?
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glutathione + cumene hydroperoxide
?
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RX + glutathione
HX + R-S-glutathione
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RX: R: aliphatic, aromatic or heterocyclic, X: sulfate, nitrite or halide, enzyme also catalyzes: the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrite, certain isomerization reactions and disulfide interchange
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additional information
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glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
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glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
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additional information
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the enzyme is active with cumene hydroperoxide. The GST A1-1 catalytic activity in steroid isomerization reactions is at least 10fold lower than the corresponding values for porcine GST A2-2, whereas the activity with 1-chloro-2,4-dinitrobenzene is approximately 8fold higher. Differences in the H-site residues of mammalian Alpha-class GSTs may explain the catalytic divergence
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additional information
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the enzyme is active with cumene hydroperoxide. The GST A1-1 catalytic activity in steroid isomerization reactions is at least 10fold lower than the corresponding values for porcine GST A2-2, whereas the activity with 1-chloro-2,4-dinitrobenzene is approximately 8fold higher. Differences in the H-site residues of mammalian Alpha-class GSTs may explain the catalytic divergence
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additional information
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additional information
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specificity
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additional information
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cantharidin has no effect on isoform SGSTalpha1 activity
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0.2
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
0.237
5-androstene-3,17-dione
pH 7.8, 30°C
0.7
5-Pregnene-3,20-dione
pH 7.8, 30°C
0.121
phenethyl isothiocyanate
pH 7.8, 30°C
0.16
trans-2-nonenal
pH 7.8, 30°C
0.091
1-chloro-2,4-dinitrobenzene
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at pH 7.5 and 30°C
0.79
glutathione
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at pH 7.5 and 30°C
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84
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
4.8
5-androstene-3,17-dione
pH 7.8, 30°C
0.01
5-Pregnene-3,20-dione
pH 7.8, 30°C
9.5
phenethyl isothiocyanate
pH 7.8, 30°C
0.155
trans-2-nonenal
pH 7.8, 30°C
99
1-chloro-2,4-dinitrobenzene
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at pH 7.5 and 30°C
141.7
glutathione
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at pH 7.5 and 30°C
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420
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
20
5-androstene-3,17-dione
pH 7.8, 30°C
16
5-Pregnene-3,20-dione
pH 7.8, 30°C
79
phenethyl isothiocyanate
pH 7.8, 30°C
1.1
trans-2-nonenal
pH 7.8, 30°C
109
1-chloro-2,4-dinitrobenzene
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at pH 7.5 and 30°C
178
glutathione
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at pH 7.5 and 30°C
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3.6 - 11.8
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with cumene hydroperoxide as substrate
7.9 - 41.1
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with 1-chloro-2,4-dinitrobenzene as substrate
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6 - 8
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more than 50% activity between pH 6.0 and 8.0
6 - 8.1
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at pH 6.0 and 8.1 about 50% of activity maximum
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20 - 40
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more than 50% activity between 20 and 40°C
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8.9
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calculated from amino acid sequence
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gene GSTA1
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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distribution in brain
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
additional information
tissue distribution of the GSTA1 mRNA, overview
brenda
additional information
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tissue distribution of the GSTA1 mRNA, overview
brenda
additional information
distribution in various tissues
brenda
additional information
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distribution in various tissues
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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GSTA1_PIG
222
0
25281
Swiss-Prot
other Location (Reliability: 5 )
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22000
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2 * 22000, SDS-PAGE
26400
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2 * 26400, isoenzyme VI, SDS-PAGE
27328
2 * 27328, electrospray ionization MS
28700
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1 * 27100 + 1 * 28700, isoenzyme I, SDS-PAGE
26000
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2 * 26000, isoenzyme VII, SDS-PAGE
26000
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1 * 26800 + 1 * 26000, isoenzyme V, SDS-PAGE
26800
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1 * 27100 + 1 * 26800, isoenzyme IV, SDS-PAGE
26800
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1 * 26800 + 1 * 26000, isoenzyme V, SDS-PAGE
27100
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1 * 27100 + 1 * 28700, isoenzyme I, SDS-PAGE
27100
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1 * 27100 + 1 * 26800, isoenzyme IV, SDS-PAGE
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?
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x * 25280, calculated from amino acid sequence
dimer
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dimer
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2 * 22000, SDS-PAGE
dimer
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2 * 26000, isoenzyme VII, SDS-PAGE
dimer
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1 * 27100 + 1 * 28700, isoenzyme I, SDS-PAGE
dimer
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2 * 26400, isoenzyme VI, SDS-PAGE
dimer
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1 * 27100 + 1 * 26800, isoenzyme IV, SDS-PAGE
dimer
2 * 27328, electrospray ionization MS
dimer
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1 * 26800 + 1 * 26000, isoenzyme V, SDS-PAGE
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loss of activity during dialysis
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recombinant isozyme GST A1-1 from Escherichia coli by ammonium sulfate fractionation, gel filtration, S-hexylglutathione affinity chromatography, ultrafiltration, and again gel filtration
5 major: I, IV, V, VI, VII and 3 minor forms
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homogeneity, 4 enzyme fractions
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Ni2+-NTA agarose column chromatography
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gene GSTA1, from ovary and testis, DNA and amino acid sequence determination and analysis, expression of isozyme GST A1-1 in Escherichia coli strain Rosetta(DE3)
expressed in Escherichia coli BL21(DE3) cells
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Williamson, G.; Ball, S.K.M.; Chan, H.W.C.
The purification of multiple forms of glutathione S-transferase from pig liver and their reaction with individual methyl linoleate hydroperoxides
Biochem. Soc. Trans.
14
1278-1279
1986
Sus scrofa
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brenda
Asaoka, K.; Takahashi, K.
Purification and properties of porcine brain glutathione S-transferases
J. Biochem.
94
1191-1199
1983
Sus scrofa
brenda
Rouimi, P.; Anglade, P.; Benzekri, A.; Costet, P.; Debrauwer, L.; Pineau, T.; Tulliez, J.
Purification and characterization of a glutathione S-transferase omega in pig: evidence for two distinct organ-specific transcripts
Biochem. J.
358
257-262
2001
Sus scrofa (Q9N1F5), Sus scrofa
brenda
Torres-Rivera, A.; Landa, A.
Glutathione transferases from parasites: a biochemical view
Acta Trop.
105
99-112
2008
Homo sapiens, Echinococcus granulosus (O16058), Rattus norvegicus (P04905), Schistosoma mansoni (P15964), Mus musculus (P24472), Schistosoma japonicum (P26624), Onchocerca volvulus (P46427), Ascaris suum (P46436), Fasciola hepatica (P56598), Sus scrofa (P80031), Clonorchis sinensis (Q1L2C7), Taenia solium (Q3ZJN3), Ancylostoma caninum (Q6J1M5), Plasmodium yoelii (Q7REH6), Wuchereria bancrofti (Q86LL8), Plasmodium falciparum (Q8MU52)
brenda
Fedulova, N.; Raffalli-Mathieu, F.; Mannervik, B.
Characterization of porcine alpha-class glutathione transferase A1-1
Arch. Biochem. Biophys.
507
205-211
2011
Sus scrofa (P51781), Sus scrofa, Sus scrofa Yorkshire pig (P51781)
brenda
Yang, X.Q.; Zhang, Y.L.
Characterization of glutathione S-transferases from Sus scrofa, Cydia pomonella and Triticum aestivum: their responses to cantharidin
Enzyme Microb. Technol.
69
1-9
2015
Sus scrofa, Triticum aestivum, Cydia pomonella
brenda
Transporter Classification Database (TCDB):
1.A.12.2.1