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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Zea mays and UniProt Accession P12653

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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.
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This record set is specific for:
Zea mays
UNIPROT: P12653
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Word Map
The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 I
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glutathione S-transferase X
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GSH S-transferase
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GSHTase-P
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S-(hydroxyalkyl)glutathione lyase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
show the reaction diagram
the enzyme uses a rapid equilibrium random sequential bi-bi mechanism with intrasubunit modulation between GSH binding site, the G-site, and electrophile binding site, the H-site, Trp12, Phe35 and Ile118 are involved in substrate binding, Phe35 is important for catalytic activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryl group transfer
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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 hide
50812-37-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
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-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
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-
-
-
?
ethacrynic acid + glutathione
?
show the reaction diagram
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-
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-
?
glutathione + 1-chloro-2,3-dinitrobenzoate
?
show the reaction diagram
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-
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-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
show the reaction diagram
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-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
show the reaction diagram
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-
-
-
?
glutathione + alachlor
?
show the reaction diagram
glutathione + butachlor
?
show the reaction diagram
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-
-
-
?
glutathione + fluorodifen
4-nitrophenol + 2-nitro-4-trifluoromethylphenol-glutathione
show the reaction diagram
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?
glutathione + terbuthylazine
?
show the reaction diagram
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?
RX + glutathione
HX + R-S-glutathione
show the reaction diagram
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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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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + alachlor
?
show the reaction diagram
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isozyme GSTI
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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no enzyme activity with potassium phosphate concentrations below 20 mM, optimal concentration 50 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
malathion
competitive
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benoxacor
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herbicide safener, activates the enzyme in shoots
cloquintocet-mexyl
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herbicide safener, activates the enzyme in shoots
fenchlorazole-ethyl
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herbicide safener, activates the enzyme in shoots
fenclorim
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herbicide safener, activates the enzyme in shoots
fluxofenim
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herbicide safener, activates the enzyme in shoots
additional information
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no enzyme activation by oxabetrinil, a herbicide safener
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 20.7
1-chloro-2,3-dinitrobenzoate
1.07 - 3
1-chloro-2,4-dinitrobenzene
0.042 - 7.23
alachlor
0.00006 - 0.0019
Ethacrynic acid
0.73 - 3.92
glutathione
0.0125 - 3.5
GSH
additional information
additional information
-
thermodynamics and kinetics of recombinant wild-type and mutant enzymes, the rate-limiting step of the reaction is viscosity-dependent product release
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011 - 0.00048
alachlor
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0297 - 0.0861
malathion
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00087
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substrate terbuthylazine
21
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GST II
66
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GST I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
assay at
6.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
assay at
30
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assay at
35
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme GST I
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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etiolated
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSTF1_MAIZE
214
0
23822
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
50000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q53A
site-directed mutagenesis, the mutant of isozyme GST I exhibits 9.2fold higher inhibition potency for the insecticide malathion compared to the wild-type enzyme, mutant immobilization by crosslinking with glutaraldehyde for formation of a malathion biosensor, overview
I118F
W12P
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turnover number with 1-chloro-2,4-dinitrobenzoate is 7.6% of the wild-type value, the ratio of turnover number to KM-value is 3.7% of the wild-type value, turnover number with ethacrynic acid is 9.5% of the wild-type value
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the presence of GSH or glycerol at 20% v/v exhibits significant stabilizing effects on the purified enzyme mutant Q53A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified mutant Q53A, 50 mM potassium phosphate buffer, pH 7.5, almost complete inactivation within 16 days, half-life of mutant inactivation is 12 days in the absence of stabilizers, or 18 days and 16 days in the presence of GSH and glycerol, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms: GST I, GST II
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native enzyme partially from shoots by ammonium sulfate fractionation and desalting
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
immobilized GST mutant Gln53Ala is used to assemble a biosensor for malathion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edwards, R.
Characterization of glutathione transferases and glutathione peroxidases in pea (Pisum sativum)
Physiol. Plant.
98
594-604
1996
Medicago sativa, Phaseolus coccineus, Phaseolus vulgaris, Pisum sativum, Trifolium repens, Triticum aestivum, Zea mays
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Manually annotated by BRENDA team
Jakoby, W.B.; Keen, J.H.
A triple-threat in detoxification: the glutathione S-transferases
Trends Biochem. Sci.
2
229-231
1977
Homo sapiens, Pisum sativum, Rattus norvegicus, Zea mays
-
Manually annotated by BRENDA team
Mozer, T.J.; Tiemeier, D.C.; Jaworski, E.G.
Purification and characterization of corn glutathione S-transferase
Biochemistry
22
1068-1072
1983
Zea mays
Manually annotated by BRENDA team
Labrou, N.E.; Kotzia, G.A.; Clonis, Y.D.
Engineering the xenobiotic substrate specificity of maize glutathione S-transferase I
Protein Eng. Des. Sel.
17
741-748
2004
Zea mays
Manually annotated by BRENDA team
Scarponi, L.; Quagliarini, E.; Del Buono, D.
Induction of wheat and maize glutathione S-transferase by some herbicide safeners and their effect on enzyme activity against butachlor and terbuthylazine
Pest Manag. Sci.
62
927-932
2006
Triticum aestivum, Zea mays
Manually annotated by BRENDA team
Labrou, N.E.; Karavangeli, M.; Tsaftaris, A.; Clonis, Y.D.
Kinetic analysis of maize glutathione S-transferase I catalysing the detoxification from chloroacetanilide herbicides
Planta
222
91-97
2005
Zea mays
Manually annotated by BRENDA team
Kapoli, P.; Axarli, I.A.; Platis, D.; Fragoulaki, M.; Paine, M.; Hemingway, J.; Vontas, J.; Labrou, N.E.
Engineering sensitive glutathione transferase for the detection of xenobiotics
Biosens. Bioelectron.
24
498-503
2008
Zea mays (P12653), Zea mays
Manually annotated by BRENDA team