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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.18 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.18 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
2.5.1.18 additional information structural and mechanistic studies on ligand binding and enzyme inhibition, overview Plasmodium falciparum
2.5.1.18 S-hexylglutathione binding structure, overview Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.18 Plasmodium falciparum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.18 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
a

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.5.1.18 glutathione S-transferase
-
 Plasmodium falciparum
2.5.1.18 GST
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.18 37
-
 assay at Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.18 6.5
-
 assay at Plasmodium falciparum