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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Mus musculus and UniProt Accession P19157
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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
-
drug-metabolizing
-
preneoplastic
-
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: Mus musculus
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
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase X
-
-
-
-
glutathione-S-transferase
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
glutathione S-transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
the mutant C169A exhibits cooperative behaviour and a ping pong mechanism whereby liberation of a proton from a reduced enzyme-glutathione complex to form an enzyme-unprotonated glutathione complex is essentially irreversible
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
1-chloro-2,3-dinitrobenzene + glutathione
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
glutathione + 1-bromo-4-nitrobenzene
bromide + 4-nitrophenyl-glutathione
-
recombinant catalytically active monoclonal antibody fragment ScFv2F3
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
recombinant catalytically active monoclonal antibody fragment ScFv2F3
-
-
?
RX + glutathione
HX + R-S-glutathione
-
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
-
-
?
RX + glutathione
HX + R-S-glutathione
-
participates in detoxification
-
-
?
additional information
?
-
-
GST isozymes play independent roles that characterize multiple processes within vomeronasal organ chemosensitivity
-
-
?
additional information
?
-
-
infection of skeletal muscle with Trichinella spiralis affects the Km of the enzyme due to alterations of the enzyme's quarternary structure, overview
-
-
?
additional information
?
-
-
the selenomethionine-labeled antibody fragment ScFv2F3 is catalytically inactive
-
-
?
additional information
?
-
-
the murine isozyme GST T1-1 is 80fold more active than the human isozyme GST T1-1
-
-
?
additional information
?
-
-
substrate specificity, overview. A major structural determinant of substrate recognition is the H-site, which binds the electrophile in proximity to the nucleophilic sulfur of the second substrate glutathione. H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1
-
-
?
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
RX + glutathione
HX + R-S-glutathione
-
participates in detoxification
-
-
?
additional information
?
-
-
GST isozymes play independent roles that characterize multiple processes within vomeronasal organ chemosensitivity
-
-
?
additional information
?
-
-
infection of skeletal muscle with Trichinella spiralis affects the Km of the enzyme due to alterations of the enzyme's quarternary structure, overview
-
-
?
additional information
?
-
-
the murine isozyme GST T1-1 is 80fold more active than the human isozyme GST T1-1
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
inhibits the mu- and pi-class GST activities in vivo by 53% and 13%, respectively, in hepatocytes and the culture medium, the enzyme activity is increased in the cell medium, overview, the inhibitory effect is completely oe partially reversible by vitamin E or 4-methylpyrazole, respectively
additional information
-
difference in sensitivity to inhibition of enzyme MI, MII and MIII
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.284
1-chloro-2,4-dinitrobenzene
-
pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3
0.455
glutathione
-
pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3
0.6
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant mutant F2:1215
0.8
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant wild-type isozyme GST-T1-1
additional information
additional information
the native enzyme and the C169A mutant exhibit MichaelisMenten kinetics, but all other thiol to alanine mutants exhibit sigmoidal kinetics to varying degrees, ping-pong kinetics of mutant C169A, overview
-
additional information
additional information
-
the native enzyme and the C169A mutant exhibit MichaelisMenten kinetics, but all other thiol to alanine mutants exhibit sigmoidal kinetics to varying degrees, ping-pong kinetics of mutant C169A, overview
-
additional information
additional information
-
biphasic kinetics of enzyme from healthy and muscle with experimental trichinellosis in presence or absence of albendazole, overview
-
additional information
additional information
-
kinetics, single-enzyme Michaelis-Menten model
-
additional information
additional information
-
steady-state kinetics of the recombinant catalytically active monoclonal antibody fragment ScFv2F3, dependence on substrate concentrations, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of recombinant His6-tagged isozyme GST T1-1, substrate 1,3-bis-(2-chloroethyl)-1-nitrosourea
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2286
1-chloro-2,4-dinitrobenzene
-
pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3
2286
glutathione
-
pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3
2.3
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant wild-type isozyme GST-T1-1
3.6
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant mutant F2:1215
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant wild-type isozyme GST-T1-1
6.3
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
pH 7.4, 37°C, recombinant mutant F2:1215
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
substrate specificities of recombinant His-tagged wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
32% of maximal activity at pH 6.5, recombinant catalytically active monoclonal antibody fragment ScFv2F3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
-
57.2% of maximal activity at 25°C, 5.6% at 60°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
higher expression of isoenzyme alpha in main olfactory tissue in comparison to vomeronasal organ
-
higher expression of isoenzyme mu in main alfactory tissue in comparison to vomeronasal organ
-
isoenzyme pi is equally expressed in both, main olfactory tissue and vomeronasal organ
-
higher expression of isoenzyme alpha in main olfactory tissue in comparison to vomeronasal organ
-
higher expression of isoenzyme mu in main alfactory tissue in comparison to vomeronasal organ
-
isoenzyme pi is equally expressed in both, main olfactory tissue and vomeronasal organ
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). GSTP1_MOUSE
210
0
23609
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
trichinellosis and of albendazole treatment influence the quaternary structure of cytosolic GST in muscles during experimental trichinellosis in mice, overview
additional information
-
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant GSTP1-1 C47A mutant, hanging drop vapour diffusion method, mixing of 0.002 ml of 7 mg/ml protein in 10 mM MES, pH 6.0, with 0.0006 ml of 30 mM S-(p-nitrobenzyl)glutathione in 50 mM MES, pH 6.0, and 0.003 ml of reservoir solution containing 20% PEG 6000 and 0.1 M sodium citrate, pH 4.0, several weeks, 20°C, X-ray diffraction structure determmintion and analysis at 1.77 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the native enzyme and the C169A mutant exhibit Michaelis-Menten kinetics, but all other thiol to alanine mutants exhibit sigmoidal kinetics to varying degrees
additional information
-
the native enzyme and the C169A mutant exhibit Michaelis-Menten kinetics, but all other thiol to alanine mutants exhibit sigmoidal kinetics to varying degrees
additional information
-
construction of the catalytically active antibody fragment ScFv2F3 by cloning of VH and VL genes of monoclonal 2F3, elicited against hapten GSH-S-DN2phBu, and sequencing from hybridoma 2F3, followed by protein engineering
additional information
-
construction of chimeric mutants F2:1215 and F5:1474 comprising sequences from the murine isozymes GST-T1-1, as well as from the isozymes GST-T1-1 and GST-T2 of Homo sapiens, the mutant F2:1215 and mutant F5:1474 show increased activity compared to the human and to the murine enzyme, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant GSTP1-1s from Escherichia coli by glutathione affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain XL1-Blue by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL1-Blue
-
recombinant expression of the His6-tagged isozyme GST T1-1 in Escherichia coli
-
the catalytically active antibody fragment ScFv2F3 is expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Warholm, M.; Jensson, H.; Tahir, M.K.; Mannervik, B.
Purification and characterization of three distinct glutathione transferases from mouse liver
Biochemistry
25
4119-4125
1986
Mus musculus
Jakoby, W.B.
Glutathione transferases: an overview
Methods Enzymol.
113
495-499
1985
Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus
Lee, C.Y.G.
Multiple forms of mouse glutathione S-transferases
Biochem. Soc. Trans.
12
30-33
1984
Mus musculus
Kitteringham, N.R.; Powell, H.; Jenkins, R.E.; Hamlett, J.; Lovatt, C.; Elsby, R.; Henderson, C.J.; Wolf, C.R.; Pennington, S.R.; Park, B.K.
Protein expression profiling of glutathione S-transferase pi null mice as a strategy to identify potential markers of resistance to paracetamol-induced toxicity in the liver
Proteomics
3
191-207
2003
Mus musculus
Green, N.; Weech, M.; Walters, E.
Localization and characterization of glutathione-S-transferase isozymes alpha, mu, and pi within the mouse vomeronasal organ
Neurosci. Lett.
375
198-202
2005
Mus musculus
Gyamfi, M.A.; Wan, Y.J.
The effect of ethanol, ethanol metabolizing enzyme inhibitors, and Vitamin E on regulating glutathione, glutathione S-transferase, and S-adenosylmethionine in mouse primary hepatocyte
Hepatol. Res.
35
53-61
2006
Mus musculus
Zhang, K.; Zang, T.Z.; Yang, W.; Sun, Y.; Mu, Y.; Liu, J.Q.; Shen, J.C.; Luo, G.M.
Single chain antibody displays glutathione S-transferase activity
J. Biol. Chem.
281
12516-12520
2006
Mus musculus
Wojtkowiak, A.; Boczo?, K.; Wandurska-Nowak, E.; Derda, M.
Evaluation of effects of albendazole on the kinetics of cytosolic glutathione transferase in skeletal muscles during experimental trichinellosis in mice
Parasitol. Res.
100
647-651
2007
Mus musculus, Mus musculus BALB/c
Cannady, E.A.; Chien, C.; Jones, T.M.; Borel, A.G.
In vitro metabolism of the epoxide substructure of cryptophycins by cytosolic glutathione S-transferase: species differences and stereoselectivity
Xenobiotica
36
659-670
2006
Canis lupus familiaris, Macaca fascicularis, Homo sapiens, Mus musculus, Rattus norvegicus, Mus musculus CD1
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)
Larsson, A.K.; Shokeer, A.; Mannervik, B.
Molecular evolution of theta-class glutathione transferase for enhanced activity with the anticancer drug 1,3-bis-(2-chloroethyl)-1-nitrosourea and other alkylating agents
Arch. Biochem. Biophys.
497
28-34
2010
Homo sapiens, Mus musculus
Shokeer, A.; Mannervik, B.
Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1
Biochim. Biophys. Acta
1800
466-473
2010
Mus musculus, Rattus norvegicus, Homo sapiens (P30711), Homo sapiens
McManus, G.; Costa, M.; Canals, A.; Coll, M.; Mantle, T.J.
Site-directed mutagenesis of mouse glutathione transferase P1-1 unlocks masked cooperativity, introduces a novel mechanism for ping pong kinetic behaviour, and provides further structural evidence for participation of a water molecule in proton abstract
FEBS J.
278
273-281
2011
Mus musculus (P19157), Mus musculus
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
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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