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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZRW8
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2.5.1.18 glutathione transferaseIUBMB 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.
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Word Map
- 2.5.1.18
- catalase
- dismutase
- sod
-
pull-down
- malondialdehyde
- carcinogenesis
-
detoxify
- hepatocytes
-
smoke
- isoenzymes
- cyp1a1
-
smoking
-
case-control
-
electrophilic
- epoxide
-
aquatic
- wistar
-
genotoxic
-
insecticide
-
chemopreventive
- gill
-
hepatocarcinogenesis
- acetylcholinesterase
-
polycyclic
-
pesticide
- hydroperoxide
-
thiobarbituric
-
hepatotoxicity
-
tbars
-
ache
-
albino
- metallothioneins
-
cigarette
-
benzoapyrene
- phenobarbital
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drug-metabolizing
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preneoplastic
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alt
- aflatoxin
- gssg
-
hepatoprotective
- schistosoma
- comet
- carboxylesterase
- mussel
-
udp-glucuronosyltransferase
-
methylation-specific
- gsh-px
-
organophosphate
- drug development
- medicine
- cyp2d6
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GSTU19
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase X
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST
GSTU26
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
glutathione S-transferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
glutathione + acrolein
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
glutathione + methacrolein
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
12-oxo-phytodienoic acid + glutathione
10-S-glutathionyl-12-oxo-phytodienoic acid + H2O
-
-
-
-
?
glutathione + (E)-2-hexenal
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 4-hydroxy-(E)-2-nonenal
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
glutathione + acrolein
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
glutathione + crotonaldehyde
?
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
harderoporphyrinogen + glutathione
harderoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
protoporphyrinogen + glutathione
protoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
P46421, Q9C8M3, Q9FUS6, Q9FUS8, Q9FUS9, Q9FUT0, Q9SHH6, Q9SHH7, Q9SHH8, Q9ZRW8, Q9ZW27, Q9ZW28, Q9ZW29
-
-
-
?
additional information
?
-
-
benoxacor, fenclorim, and fluxofenim do not protect the plant from herbicide injury but induce RNA expression of the glutathione-conjugate transporters encoded by genes AtMRP1, AtMRP2, AtMRP3, and AtMRP4
-
-
?
additional information
?
-
-
no activity with 4-nitrobenzylchloride
-
-
?
additional information
?
-
-
no activity with 4-nitrobenzylchloride, GSTF9 also shows glutathione peroxidase activity, EC 1.11.1.9, overview
-
-
?
additional information
?
-
three recombinant theta class GSTs, GSTTs, show conserved activities as hydroperoxide-reducing glutathione peroxidases
-
-
?
additional information
?
-
-
glutathione conjugation reactions are often freely reversible, formation of unstable glutathionylated natural products in plants, the detection is difficult, overview
-
-
?
additional information
?
-
-
overexpressed in bacteria, family members GSTF2 and GSTF3 bind a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. GSTF2 also selectively binds the indole-derived phytoalexin camalexin, as well as the flavonol quercetin-3-O-rhamnoside, recombinant GSTF2 ligand binding studies and kinetics, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
12-oxo-phytodienoic acid + glutathione
10-S-glutathionyl-12-oxo-phytodienoic acid + H2O
-
-
-
-
?
harderoporphyrinogen + glutathione
harderoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
protoporphyrinogen + glutathione
protoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
additional information
?
-
-
benoxacor, fenclorim, and fluxofenim do not protect the plant from herbicide injury but induce RNA expression of the glutathione-conjugate transporters encoded by genes AtMRP1, AtMRP2, AtMRP3, and AtMRP4
-
-
?
additional information
?
-
-
glutathione conjugation reactions are often freely reversible, formation of unstable glutathionylated natural products in plants, the detection is difficult, overview
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of GSTU19 is induced in roots by herbicide safeners benoxacor, fenclorim, and fluxofenim
-
additional information
-
gene GSTF9 is not influenced by the treatments with chloroacetanilide herbicides alachlor and metolachlor and the safener benoxacor, and exposure to low temperatures, and is constitutively expressed, overview
-
additional information
-
gene GSTU26 expression is induced by the chloroacetanilide herbicides alachlor and metolachlor and the safener benoxacor, and after exposure to low temperatures, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
isothermal titration calorimetry reveals high-affinity binding for GSTF2 and GSTF3, which is enhanced in the presence of glutathione and by the other heterocyclic ligands, and allosteric enhancement in glutathione-conjugating activity
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
purified protein with poly(His) tag, with 12-oxo-phytodienoic acid as substrate, at pH 6.0 and 25°C
3.83
purified protein with poly(His) tag, with acrolein as substrate, at pH 6.0 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
organ-specific expression of genes GSTU19 and GSTF2
additional information
-
plant-specific phi class of glutathione transferases, GSTFs, are often highly stress-inducible and expressed in a tissue-specific manner
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
subcellular localization of members of the Arabidopsis thaliana GST superfamily, differential targeting, overview
-
through alternative splicing, two of these GSTTs form fusions with Myb transcription factor-like domains, discrete localization within the nucleus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme keeps the acrolein level low in plant cells
evolution
-
the enzyme belongs to the soluble plant GST superfamily of dimeric enzymes, isozymes classes, overview. Dehydroascorbate reductase and tetrachlorohydroquinone dehalogenase-like proteins also belong to the GST superfamily
malfunction
-
isozymes AtGSTs F11, F12, F14 and U14, in which the catalytic serine is replaced by a non-proton abstracting residue, show abolished transferase activity
metabolism
-
GST reaction products as metabolic intermediates, e.g. delivering the sullfur in the compounds, possible role for glutathione and GSTs in sulfur incorporation, detailed overview
physiological function
additional information
-
where GSTs are involved in conjugating acceptors with GSH, there is an absolute requirement for the conserved serine residue within the active site, as it promotes the formation of the thiolate anion of GSH. In some family members this serine is replaced with a cysteine, e.g. promoting disulfide exchange reactions in the GSTL
physiological function
through alternative splicing, two of these GSTTs form fusions with Myb transcription factor-like domains, discrete localization within the nucleus, possibly serving role in reducing nucleic acid hydroperoxides or in signalling
physiological function
-
GSTF2 and GSTF3 may have roles in regulating the binding and transport of defence-related compounds in planta
physiological function
-
GSTs functioning in the transport of secondary metabolites, e.g. of the electrophilic oxylipins. Pi class GSTs have assumed such roles in modulating the activity of Jun NH2-terminal kinase through protein-protein interactions. Tau class protein AtGSTU20 is a binding partner of the far-red insensitive 219 protein, such that alterations in its expression give rise to an altered growth phenotype under continuous far-red light. AtGSTF12, in which the catalytic serine is replaced by a non-proton abstracting residue resulting in abolished transferase activity, is necessary for correct anthocyanin pigment formation in developing Arabidopsis seeds, although their function is not related to GSH conjugation. Sometimes, following GST action, S-glutathionylated xenobiotics are imported into the vacuole by ATP-binding cassette (ABC) transporter proteins. In the GST family members where the catalytic serine is replace with a cysteine, the GSTs show the ability to co-ordinately bind hydrophobic ligands in close proximity to the reactive thiol of GSH
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GSTUJ_ARATH
219
0
25651
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
molecular modeling of the GSTZ substrate superimposed enzyme using the apoform crystal structure of AtGSTZ monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K83E
-
random mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
L147F
-
random mutagenesis, the mutant shows 47.7% reduced activity compared to the wild-type enzyme
Q102R
-
random mutagenesis, the mutant shows 68.4% reduced activity compared to the wild-type enzyme
additional information
additional information
enzyme overexpression after induction by isothiocyanates leads to a growth arrest and leaf bleaching phenotype with electrolyt leakage, overview
additional information
-
enzyme overexpression after induction by isothiocyanates leads to a growth arrest and leaf bleaching phenotype with electrolyt leakage, overview
additional information
-
mutant enzyme inactivation mechanism, molecular modeling, mutations resulting in inactivation of the enzyme are found in or near the binding pocket, whereas mutations resulting in partial inactivation are distant from both substrates, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSTrap 4B column chromatography, HiTrap Q column chromatography, and DEAE-Sepharose column chromatography
Strep-Tactin Sepharose column chromatography and Superdex S200 gel filtration
recombinant N-terminally Strep-tagged AtGSTF2 and AtGSTF3 from Escherichia coli by affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
correlation of expression of GST family members with alterations in the transcription of other genes, expression patterns, overview
-
expressed in Escherichia coli BL21 cells
expression of N-terminally Strep-tagged AtGSTF2 and AtGSTF3 in Escherichia coli, expression of untagged GSTF2
-
functional expression of 41 GST genes in Escherichia coli strain Tuner(DE3), phylogenetic tree, expression of theta class GSTs as GFP-fusion proteins in Nicotiana benthamiana peroxisomes via the Agrobacterium tumefaciens transfection system. Through alternative splicing, two of these GSTTs form fusions with Myb transcription factor-like domains. Examination of one of these variants showed discrete localization within the nucleus, possibly serving a role in reducing nucleic acid hydroperoxides or in signalling
gene GSTF9, encoding a tau class isozyme, DNA and amino acid determination and analysis, genomic and phylogenetic analysis, overview, expression in Escherichia coli, expression analysis
-
gene GSTU26, encoding a phi class isozyme, DNA and amino acid determination and analysis, genomic and phylogenetic analysis, overview, expression in Escherichia coli, expression analysis
-
GSTZ, library screening, cloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
methyl isothiocyanate, allyl isothiocyanate, and phenethylisothiocyanate induce the enzyme expression, especially of isozyme GSTU19, inhibit plant growth, and induce severe bleaching in the rosette leaves. The bleaching is concomitant with the elevation of electrolyte leakage and the generation of hydrogen peroxide
plant-specific phi class of glutathione transferases, GSTFs, are often highly stress-inducible and expressed in a tissue-specific manner
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nutricati, E.; Miceli, A.; Blando, F.; De Bellis, L.
Characterization of two Arabidopsis thaliana glutathione S-transferases
Plant Cell Rep.
25
997-1005
2006
Arabidopsis thaliana
DeRidder, B.P.; Goldsbrough, P.B.
Organ-specific expression of glutathione S-transferases and the efficacy of herbicide safeners in Arabidopsis
Plant Physiol.
140
167-175
2006
Arabidopsis thaliana
Chen, X.; Liu, J.; Yang, P.; Chen, D.
Identifying functional residues in Arabidopsis thaliana zeta class glutathione S-transferase through screening inactive point mutants
Biochemistry
75
110-114
2010
Arabidopsis thaliana
Dixon, D.P.; Hawkins, T.; Hussey, P.J.; Edwards, R.
Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily
J. Exp. Bot.
60
1207-1218
2009
Arabidopsis thaliana (Q9FUS8)
Hara, M.; Yatsuzuka, Y.; Tabata, K.; Kuboi, T.
Exogenously applied isothiocyanates enhance glutathione S-transferase expression in Arabidopsis but act as herbicides at higher concentrations
J. Plant Physiol.
167
643-649
2010
Arabidopsis thaliana (Q9ZRW8), Arabidopsis thaliana
Dixon, D.P.; Sellars, J.D.; Edwards, R.
The Arabidopsis phi class glutathione transferase AtGSTF2: binding and regulation by biologically active heterocyclic ligands
Biochem. J.
438
63-70
2011
Arabidopsis thaliana
Dixon, D.P.; Skipsey, M.; Edwards, R.
Roles for glutathione transferases in plant secondary metabolism
Phytochemistry
71
338-350
2010
Arabidopsis thaliana
Mano, J.; Ishibashi, A.; Muneuchi, H.; Morita, C.; Sakai, H.; Biswas, M.S.; Koeduka, T.; Kitajima, S.
Acrolein-detoxifying isozymes of glutathione transferase in plants
Planta
245
255-264
2017
Spinacia oleracea, Arabidopsis thaliana (Q9ZRW8), Arabidopsis thaliana
Mano, J.; Kanameda, S.; Kuramitsu, R.; Matsuura, N.; Yamauchi, Y.
Detoxification of reactive carbonyl species by glutathione transferase tau isozymes
Front. Plant Sci.
10
487
2019
Arabidopsis thaliana (P46421), Arabidopsis thaliana (Q9C8M3), Arabidopsis thaliana (Q9FUS6), Arabidopsis thaliana (Q9FUS8), Arabidopsis thaliana (Q9FUS9), Arabidopsis thaliana (Q9FUT0), Arabidopsis thaliana (Q9SHH6), Arabidopsis thaliana (Q9SHH7), Arabidopsis thaliana (Q9SHH8), Arabidopsis thaliana (Q9ZRW8), Arabidopsis thaliana (Q9ZW27), Arabidopsis thaliana (Q9ZW28), Arabidopsis thaliana (Q9ZW29), Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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