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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Plasmodium vivax and UniProt Accession Q0ZS46
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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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- 2.5.1.18
- catalase
- dismutase
- sod
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pull-down
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- carcinogenesis
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detoxify
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smoke
- isoenzymes
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smoking
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case-control
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electrophilic
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aquatic
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genotoxic
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insecticide
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chemopreventive
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hepatocarcinogenesis
- acetylcholinesterase
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polycyclic
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pesticide
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thiobarbituric
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hepatotoxicity
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tbars
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ache
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albino
- metallothioneins
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cigarette
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benzoapyrene
- phenobarbital
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drug-metabolizing
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preneoplastic
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alt
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hepatoprotective
- schistosoma
- comet
- carboxylesterase
- mussel
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udp-glucuronosyltransferase
-
methylation-specific
- gsh-px
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organophosphate
- drug development
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- cyp2d6
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Plasmodium vivax
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
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
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 + 1,2-dichloro-4-nitrobenzene
?
low activity compared to 1-chloro-2,4-dinitrobenzene
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
preferred substrate
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + ethacrynic acid
?
low activity compared to 1-chloro-2,4-dinitrobenzene
-
-
?
additional information
?
-
the enzyme is essential for parasite survival by protecting the parasite against oxidative stress and buffering the detoxification of heme-binding compounds
-
-
?
additional information
?
-
-
the enzyme is essential for parasite survival by protecting the parasite against oxidative stress and buffering the detoxification of heme-binding compounds
-
-
?
additional information
?
-
2-nitrophenyl acetate, bromosulfophthalein, and cumene hydroperoxide are poor substrates, overview
-
-
?
additional information
?
-
-
2-nitrophenyl acetate, bromosulfophthalein, and cumene hydroperoxide are poor substrates, overview
-
-
?
additional information
?
-
the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium, three-dimensional modeling, overview
-
-
?
additional information
?
-
-
the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium, three-dimensional modeling, 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
additional information
?
-
the enzyme is essential for parasite survival by protecting the parasite against oxidative stress and buffering the detoxification of heme-binding compounds
-
-
?
additional information
?
-
-
the enzyme is essential for parasite survival by protecting the parasite against oxidative stress and buffering the detoxification of heme-binding compounds
-
-
?
additional information
?
-
the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium, three-dimensional modeling, overview
-
-
?
additional information
?
-
-
the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium, three-dimensional modeling, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
presence of salts effectively inhibits PvGST enzymatic activity by quenching the nucleophilicity of the thiolate anion of GSH, relative decrease in descending order MgCl2, MgSO4, NaCl, Na2SO4
-
additional information
-
presence of salts effectively inhibits PvGST enzymatic activity by quenching the nucleophilicity of the thiolate anion of GSH, relative decrease in descending order MgCl2, MgSO4, NaCl, Na2SO4
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.58
purified recombinant enzyme, substrate 1,2-dichloro-4-nitrobenzene
34.7
purified recombinant enzyme, substrate 1-chloro-2,4-dinitrobenzene
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). GST_PLAVI
205
0
24212
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
50000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
unfolding behavior of Plasmodium vivax GST is significantly different from Plasmodium falciparum GST, the unfolding pathway of Plasmodium vivax GST is non-cooperative with stabilization of an inactive dimeric intermediate. The absence of any compact folded monomeric intermediate during the unfolding transition suggests that inter-subunit interactions play an important role in stabilizing the protein, overview. Three-dimensional modeling, overview
additional information
-
unfolding behavior of Plasmodium vivax GST is significantly different from Plasmodium falciparum GST, the unfolding pathway of Plasmodium vivax GST is non-cooperative with stabilization of an inactive dimeric intermediate. The absence of any compact folded monomeric intermediate during the unfolding transition suggests that inter-subunit interactions play an important role in stabilizing the protein, overview. Three-dimensional modeling, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme immobilization by glutaraldehyde cross-linking, overview
additional information
-
enzyme immobilization by glutaraldehyde cross-linking, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unfolding behavior of Plasmodium vivax GST is significantly different from Plasmodium falciparum GST, the unfolding pathway of Plasmodium vivax GST is non-cooperative with stabilization of an inactive dimeric intermediate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography, recombinant enzyme from Escherichia coli strain DH5alpha by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gst, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain M15
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the enzyme is a target for drug development against the parasite
drug development
glutathione S-transferases of Plasmodium parasites are potential targets for antimalarial drug and vaccine development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Na, B.K.; Kang, J.M.; Kim, T.S.; Sohn, W.M.
Plasmodium vivax: molecular cloning, expression and characterization of glutathione S-transferase
Exp. Parasitol.
116
414-418
2007
Plasmodium vivax (Q0ZS46), Plasmodium vivax
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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Release 2023.1 (January 2023)
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