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Literature summary for 2.5.1.18 extracted from

  • 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 (2006), Protein Sci., 15, 281-289.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes in Escherichia coli Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
C101A site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme Plasmodium falciparum
C86A site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme Plasmodium falciparum
K15E site-directed mutagenesis, the mutant shows altered ligand binding compared to the wild-type enzyme Plasmodium falciparum
Q71E site-directed mutagenesis, the mutant shows altered ligand binding compared to the wild-type enzyme Plasmodium falciparum
Y211F site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme Plasmodium falciparum
Y9F site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
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 Plasmodium falciparum
additional information structural and mechanistic studies on ligand binding and enzyme inhibition, overview Plasmodium falciparum
S-hexylglutathione binding structure, overview Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
RX + glutathione = HX + R-S-glutathione substrate binding: Tyr9 is responsible for the deprotonation of GSH and Lys15, but also Gln71 are involved, active site and substrate binding structure, overview Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1-chloro-2,4-dinitrobenzene substrate binding structure, overview Plasmodium falciparum chloride + 2,4-dinitrophenyl-glutathione
-
?
additional information artemisinin is no substrate for glutathione transferase activity but for peroxidase activity, as is cumene hydroperoxide Plasmodium falciparum ?
-
?

Subunits

Subunits Comment Organism
More tertiary and quaternary structure of the enzyme with bound S-hexylglutathione Plasmodium falciparum
tetramer a tetramer that dissociates into dimers in the presence of glutathione Plasmodium falciparum

Synonyms

Synonyms Comment Organism
glutathione S-transferase
-
Plasmodium falciparum
GST
-
Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Plasmodium falciparum