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Literature summary for 2.5.1.18 extracted from

  • Tripathi, T.; Na, B.K.; Sohn, W.M.; Becker, K.; Bhakuni, V.
    Structural, functional and unfolding characteristics of glutathione S-transferase of Plasmodium vivax (2009), Arch. Biochem. Biophys., 487, 115-122.
    View publication on PubMed

Application

Application Comment Organism
drug development glutathione S-transferases of Plasmodium parasites are potential targets for antimalarial drug and vaccine development Plasmodium vivax

Protein Variants

Protein Variants Comment Organism
additional information enzyme immobilization by glutaraldehyde cross-linking, overview Plasmodium vivax

General Stability

General Stability Organism
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 Plasmodium vivax

Inhibitors

Inhibitors Comment Organism Structure
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 Plasmodium vivax

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
x * 25000, recombinant enzyme, SDS-PAGE Plasmodium vivax
50000
-
recombinant dimeric enzyme, gel filtration Plasmodium vivax
100000
-
recombinant tetrameric enzyme, gel filtration Plasmodium vivax

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium vivax the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium, three-dimensional modeling, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium vivax Q0ZS46
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1-chloro-2,4-dinitrobenzene
-
Plasmodium vivax S-(2,4-dinitrophenyl)glutathione + HCl
-
?
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 Plasmodium vivax ?
-
?

Subunits

Subunits Comment Organism
dimer or tetramer x * 25000, recombinant enzyme, SDS-PAGE Plasmodium vivax
More 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 Plasmodium vivax

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Plasmodium vivax

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Plasmodium vivax