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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: Oryza sativa 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,
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tau class glutathione S-transferase
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tau class glutathione transferase
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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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GSTF3
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phi class isozyme
GSTF5
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phi class isozyme
GSTU3
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tau class isozyme
GSTU4
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tau class isozyme
GSTU5
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tau class isozyme
S-(hydroxyalkyl)glutathione lyase
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GSTU17
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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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glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
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-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
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-
-
?
glutathione + 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole
?
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-
-
?
glutathione + 4-nitrobenzo-2-oxa-1,3-diazole
?
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-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + 4-nitrobenzyl-glutathione
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-
-
?
glutathione + 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
?
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-
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?
glutathione + cumene hydroperoxide
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glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
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-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
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-
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?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
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?
glutathione + acetochlor
?
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?
glutathione + alachlor
?
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?
glutathione + cumene hydroperoxide
?
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?
glutathione + ethacrynic acid
?
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?
glutathione + fenchlorim
?
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?
glutathione + fluorodifen
4-nitrophenol + (2-nitro-4-trifluoromethylphenyl)glutathione
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?
glutathione + metolachlor
?
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?
glutathione + petrilachlor
?
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?
glutathione + pretilachlor
?
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?
additional information
?
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glutathione + cumene hydroperoxide
?
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?
glutathione + cumene hydroperoxide
?
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?
additional information
?
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no activity with 1,2-dichloro-4-nitrobenzene, 4-nitrophenyl acetate, and ethacrynic acid
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?
additional information
?
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no activity with 1,2-dichloro-4-nitrobenzene, 4-nitrophenyl acetate, and ethacrynic acid
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additional information
?
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no activity toward 1,2-dichloro-4-nitrobenzene, 4-nitrophenyl acetate and ethacrynic acid
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additional information
?
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no activity toward 1,2-dichloro-4-nitrobenzene, 4-nitrophenyl acetate and ethacrynic acid
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additional information
?
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no activity with atrazine and acifluorofen
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?
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Cu2+
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about 52% inhibition at 0.008 mM
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0.324 - 3.866
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
0.324
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
pH 7.4, 37°C
0.058 - 0.743
glutathione
0.324
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
wild type enzyme, at 25°C, pH not specified in the publication
0.47 - 1
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme Y113A, at 25°C, pH not specified in the publication
0.781
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme N109A, at 25°C, pH not specified in the publication
0.882
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F116A, at 25°C, pH not specified in the publication
1.117
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme W161A, at 25°C, pH not specified in the publication
1.487
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme L112A, at 25°C, pH not specified in the publication
3.661
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme M17A, at 25°C, pH not specified in the publication
3.866
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F162A, at 25°C, pH not specified in the publication
0.058
glutathione
pH 7.4, 37°C
0.058
glutathione
wild type enzyme, at 25°C, pH not specified in the publication
0.12
glutathione
mutant enzyme Y113A, at 25°C, pH not specified in the publication
0.166
glutathione
mutant enzyme F116A, at 25°C, pH not specified in the publication
0.192
glutathione
mutant enzyme N109A, at 25°C, pH not specified in the publication
0.221
glutathione
mutant enzyme W161A, at 25°C, pH not specified in the publication
0.307
glutathione
mutant enzyme L112A, at 25°C, pH not specified in the publication
0.36
glutathione
mutant enzyme F162A, at 25°C, pH not specified in the publication
0.743
glutathione
mutant enzyme M17A, at 25°C, pH not specified in the publication
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0.257 - 1.75
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
0.257
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
pH 7.4, 37°C
0.196 - 0.946
glutathione
0.257
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
wild type enzyme, at 25°C, pH not specified in the publication
0.266
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme N109A, at 25°C, pH not specified in the publication
0.277
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme Y113A, at 25°C, pH not specified in the publication
0.512
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F116A, at 25°C, pH not specified in the publication
0.809
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme M17A, at 25°C, pH not specified in the publication
0.999
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme W161A, at 25°C, pH not specified in the publication
1.573
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F162A, at 25°C, pH not specified in the publication
1.75
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme L112A, at 25°C, pH not specified in the publication
0.196
glutathione
mutant enzyme N109A, at 25°C, pH not specified in the publication
0.22
glutathione
mutant enzyme Y113A, at 25°C, pH not specified in the publication
0.264
glutathione
pH 7.4, 37°C
0.264
glutathione
wild type enzyme, at 25°C, pH not specified in the publication
0.322
glutathione
mutant enzyme F116A, at 25°C, pH not specified in the publication
0.387
glutathione
mutant enzyme M17A, at 25°C, pH not specified in the publication
0.421
glutathione
mutant enzyme F162A, at 25°C, pH not specified in the publication
0.573
glutathione
mutant enzyme W161A, at 25°C, pH not specified in the publication
0.946
glutathione
mutant enzyme L112A, at 25°C, pH not specified in the publication
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0.221 - 1.177
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
0.013
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
pH 7.4, 37°C
0.076 - 4.552
glutathione
0.221
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme M17A, at 25°C, pH not specified in the publication
0.341
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme N109A, at 25°C, pH not specified in the publication
0.407
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F162A, at 25°C, pH not specified in the publication
0.581
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme F116A, at 25°C, pH not specified in the publication
0.589
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme Y113A, at 25°C, pH not specified in the publication
0.793
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
wild type enzyme, at 25°C, pH not specified in the publication
0.894
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme W161A, at 25°C, pH not specified in the publication
1.177
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
mutant enzyme L112A, at 25°C, pH not specified in the publication
0.076
glutathione
pH 7.4, 37°C
0.521
glutathione
mutant enzyme M17A, at 25°C, pH not specified in the publication
1.019
glutathione
mutant enzyme N109A, at 25°C, pH not specified in the publication
1.17
glutathione
mutant enzyme F162A, at 25°C, pH not specified in the publication
1.579
glutathione
mutant enzyme L112A, at 25°C, pH not specified in the publication
1.842
glutathione
mutant enzyme Y113A, at 25°C, pH not specified in the publication
1.942
glutathione
mutant enzyme F116A, at 25°C, pH not specified in the publication
2.588
glutathione
mutant enzyme W161A, at 25°C, pH not specified in the publication
4.552
glutathione
wild type enzyme, at 25°C, pH not specified in the publication
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0.203
GSTU17, substrate 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
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5.5 - 8.5
activity range of GSTU17
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UniProt
brenda
GSTU17; isozyme GSTU17
UniProt
brenda
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low expression of GSTU17
brenda
high expression of GSTU17 in mature, lower in young leaves, no expression in immature leaves
brenda
low expression of GSTU17
brenda
low expression of GSTU17
brenda
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young and mature
brenda
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brenda
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brenda
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brenda
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brenda
additional information
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expression patterns of rice GST genes in various tissues/organs and developmental stages, overview
brenda
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etiolated
brenda
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apical meristem
brenda
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brenda
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metabolism
the classical phase II detoxification glutathione transferases are key metabolic enzymes that catalyze the conjugation of glutathione to various electrophilic compounds
physiological function
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overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses, role of GSTs in mediating crosstalk between various stress and hormone response pathways
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25180
x * 25180, GSTU17, sequence calculation
25000
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1 * 25000 + 1 * 28000, GST II-III, SDS-PAGE
28000
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1 * 25000 + 1 * 28000, GST II-III, SDS-PAGE
30000
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2 * 30000, GST I, SDS-PAGE
45000 - 60000
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gel filtration
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?
x * 25000, SDS-PAGE
?
x * 25180, GSTU17, sequence calculation
dimer
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2 * 30000, GST I, SDS-PAGE
dimer
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1 * 25000 + 1 * 28000, GST II-III, SDS-PAGE
additional information
structure homology modeling
additional information
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structure homology modeling
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E68A
the mutant retains activity toward 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole, 1-chloro-2,4-dinitrobenzene and 4-nitrobenzyl chloride, but its activities drop significantly compared to the wild type enzyme
F116A
the mutant shows reduced catalytic efficiency toward glutathione and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
F162A
the mutant shows reduced catalytic efficiency toward glutathione and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
K42A
the mutant shows 10% of wild type activity
L112A
the mutant shows reduced catalytic efficiency toward glutathione and increased catalytic efficiency toward 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
M17A
the mutant shows reduced catalytic efficiency toward glutathione and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
N109A
the mutant shows reduced catalytic efficiency toward glutathione and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
S69A
the mutant loses activity to 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole while it retains 31% of the activity toward 1-chloro-2,4-dinitrobenzene and 7-8% of the activity toward 4-nitrobenzyl chloride, respectively, compared with the wild type enzyme
V56A
the mutant loses activity to 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole while it retains 21% of the activity toward 1-chloro-2,4-dinitrobenzene and 7-8% of the activity toward 4-nitrobenzyl chloride, respectively, compared with the wild type enzyme
W161A
the mutant shows reduced catalytic efficiency toward glutathione and increased catalytic efficiency toward 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
Y113A
the mutant shows reduced catalytic efficiency toward glutathione and 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole as compared to the wild type enzyme
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25 - 55
the enzyme retains about 85, 99, 95 and 65% activity after 15 min at 25, 35, 45 and 55°C, respectively. The enzyme is inactivated at 65°C
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Ni-Sepharose column chromatography
glutathione Sepharose column chromatography
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homogeneity, 2 isoenzymes: GST I-I and GST II-III
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expressed in Escherichia coli BL21(DE3) cells
tau class GST gene OsGSTU17, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged GSTU17 in Escherichia coli strain Bl21
79 genes encoding GSTs, DNA and amino acid sequence determination and analysis, sequence compariosns and phylogenetic analysis, detailed overview
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expressed in Escherichia coli
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at least 31 GST genes show response to plant hormones auxin and cytokinin, differential expression of quite a large number of GST genes during various abiotic stress, arsenate stress and biotic stress conditions, detailed overview
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Deng, F.; Hatzios, K.K.
Purification and characterization of two glutathione S-transferase isozymes from Indica-type rice involved in herbicide detoxification
Pestic. Biochem. Physiol.
72
10-23
2002
Oryza sativa
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brenda
Cho, H.Y.; Kong, K.H.
Study on the biochemical characterization of herbicide detoxification enzyme, glutathione S-transferase
Biofactors
30
281-287
2007
Homo sapiens, Oryza sativa
brenda
Jain, M.; Ghanashyam, C.; Bhattacharjee, A.
Comprehensive expression analysis suggests overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses
BMC Genomics
11
73
2010
Oryza sativa
brenda
Yang, X.; Sun, W.; Liu, J.P.; Liu, Y.J.; Zeng, Q.Y.
Biochemical and physiological characterization of a tau class glutathione transferase from rice (Oryza sativa)
Plant Physiol. Biochem.
47
1061-1068
2009
Oryza sativa (Q93WY5), Oryza sativa
brenda
Yang, X.; Wei, J.; Wu, Z.; Gao, J.
Effects of substrate-binding site residues on the biochemical properties of a tau class glutathione S-transferase from Oryza sativa
Genes (Basel)
11
25
2019
Oryza sativa (Q93WY5), Oryza sativa
brenda
Dobritzsch, D.; Grancharov, K.; Hermsen, C.; Krauss, G.J.; Schaumloeffel, D.
Inhibitory effect of metals on animal and plant glutathione transferases
J. Trace Elem. Med. Biol.
57
48-56
2020
Armoracia rusticana, Astacus astacus, Brassica juncea, Oryctolagus cuniculus, Lemna minor, Meleagris gallopavo, Mus musculus, Oncorhynchus mykiss, Oreochromis mossambicus, Oryza sativa, Pacifastacus leniusculus, Picea abies, Pleuronectes platessa, Populus sp., Pelophylax ridibundus, Rattus norvegicus, Typha latifolia, Rhabdosargus sarba, Chelon saliens, Protaetia brevitarsis, Alburnus tarichi, Salvelinus alpinus, Siganus canaliculatus, Laeonereis acuta
brenda
Transporter Classification Database (TCDB):
1.A.12.2.1