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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Plasmodium falciparum and UniProt Accession Q8MU52

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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:
Plasmodium falciparum
UNIPROT: Q8MU52
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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RX
+
glutathione
=
HX
+
R-S-glutathione
+
=
+
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-transferase
Q8MU52
-
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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
show the reaction diagram
substrate binding: Tyr9 is responsible for the deprotonation of GSH and Lys15, but also Gln71 are involved, active site and substrate binding structure, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryl group transfer
-
-
-
-
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
-
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
Q8MU52
-
-
-
?
glutathione + ethacrynic acid
?
show the reaction diagram
Q8MU52
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
show the reaction diagram
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
artemisinin is no substrate for glutathione transferase activity but for peroxidase activity, as is cumene hydroperoxide
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Amino-4-{[4-({4-chloro-6-[(2-sulfophenyl)amino]-1,3,5-triazin-2-yl}amino)-3-sulfophenyl]amino}-9,10-dioxo-9,10-dihydro-2-anthracenesulfonic acid
Q8MU52
-
haematin
Q8MU52
-
protoporphyrin IX
Q8MU52
-
ferriprotoporphyrin IX
-
in presence of glutathione, GST serves as ligand for parasitotoxic ferriprotoporphyrin IX with a high- and a low-affinity binding site, uncompetitive inhibition type, overview
S-hexylglutathione
-
binding structure, overview
additional information
-
structural and mechanistic studies on ligand binding and enzyme inhibition, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
1-chloro-2,4-dinitrobenzene
Q8MU52
Km above 2.0 mM
0.16
glutathione
Q8MU52
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
Cibacron blue 3GA
Q8MU52
-
0.01
haematin
Q8MU52
-
0.01
protoporphyrin IX
Q8MU52
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Q8MU52
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
Q8MU52
2 * 25000
104000
-
gel filtration
26000
-
4 * 26000, gel filtration, inactive enzyme form under native conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Q8MU52
2 * 25000
dimer
-
active enzyme form, in the presence of 2 mM glutathione
tetramer
additional information
-
tertiary and quaternary structure of the enzyme with bound S-hexylglutathione
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type GST in complex with inhibitor S-hexylglutathione, 22°C, hanging drop vapour diffusion method, from 60 mM CaCl2, 30 mM HEPES, pH 7.5, 8.4% PEG 400, 3.4 mg GST/ml, and 1.4 mM S-hexylglutathione, the reservoir solution contains 150 mM CaCl2, 75 mM HEPES, pH 7.5, and 21% PEG 400, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
recombinant enzyme expressed in bacterial cells, hanging-drop vapour diffusion. X-ray intensity data to 2.8 A resolution are collected from an orthorhombic crystal form with unit-cell parameters a = 62.2, b = 88.3, c = 75.3 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C101A
-
site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme
C86A
-
site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme
K15E
-
site-directed mutagenesis, the mutant shows altered ligand binding compared to the wild-type enzyme
Q71E
-
site-directed mutagenesis, the mutant shows altered ligand binding compared to the wild-type enzyme
Y211F
-
site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme
Y9F
-
site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
for the GST dimer, the secondary structure is stable between pH 5.0 and 8.0, decrease in pH below 5.0 or increase in pH above 8.0 results in denaturation of the enzyme as indicated by a significant loss in secondary structure, at pH 4.0 or below and pH 10.0 almost complete loss of secondary structure is observed, for the GST tetramer a sigmoidal dependence of the loss of secondary structure on the pH value is observed, between pH 10.0 and 6.0 no alteration is determined, decrease in pH below 6.0 results in loss of secondary structure, even at a pH as low as 3.0 only a partial loss of secondary structure of about 50% is observed
685844
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
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overexpression of wild-type and mutant enzymes in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Burmeister, C.; Perbandt, M.; Betzel, C.; Walter, R.D.; Liebau, E.
Crystallization and preliminary X-ray diffraction studies of the glutathione S-transferase from Plasmodium falciparum
Acta Crystallogr. Sect. D
59
1469-1471
2003
Plasmodium falciparum
Manually annotated by BRENDA team
Hiller, N.; Fritz-Wolf, K.; Deponte, M.; Wende, W.; Zimmermann, H.; Becker, K.
Plasmodium falciparum glutathione S-transferase - structural and mechanistic studies on ligand binding and enzyme inhibition
Protein Sci.
15
281-289
2006
Plasmodium falciparum
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Tripathi, T.; Rahlfs, S.; Becker, K.; Bhakuni, V.
Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase
BMC Struct. Biol.
7
67
2007
Plasmodium falciparum
Manually annotated by BRENDA team