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Literature summary for 2.5.1.18 extracted from

  • Tripathi, T.; Rahlfs, S.; Becker, K.; Bhakuni, V.
    Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase (2007), BMC Struct. Biol., 7, 67.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli M15 cells Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
4 * 26000, gel filtration, inactive enzyme form under native conditions Plasmodium falciparum
104000
-
gel filtration Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose chromatography Plasmodium falciparum

Subunits

Subunits Comment Organism
dimer active enzyme form, in the presence of 2 mM glutathione Plasmodium falciparum
tetramer 4 * 26000, gel filtration, inactive enzyme form under native conditions Plasmodium falciparum

Synonyms

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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 Plasmodium falciparum