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Literature summary for 2.5.1.18 extracted from

  • Jiang, Z.; Arner, E.S.J.; Mu, Y.; Johansson, L.; Shi, J.; Zhao, S.; Liu, S.; Wang, R.; Zhang, T.; Yan, G.; Liu, J.; Shen, J.; Luo, G.
    Expression of selenocysteine-containing glutathione S-transferase in Escherichia coli (2004), Biochem. Biophys. Res. Commun., 321, 94-101.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
production of recombinant selenoproteins with internal selenocysteine residues in Escherichia col, introduction of a variant bacterial-type selenocysteine insertion sequence element which afforded substitution with selenocysteine for the catalytic Tyr residue in the active site of the enzyme Schistosoma japonicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.063
-
GSH wild-type enzyme Schistosoma japonicum
0.57
-
GSH selenoenzyme Schistosoma japonicum

Metals/Ions

Metals/Ions Comment Organism Structure
selenium production of recombinant selenoproteins with internal selenocysteine residues in Escherichia coli. Introduction of a selenocysteine residue into the catalytic site of glutathione S-transferase is not sufficient to induce glutathione peroxidase activity in spite of a maintained glutathione-binding capacity Schistosoma japonicum

Organism

Organism UniProt Comment Textmining
Schistosoma japonicum
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
sjGST
-
Schistosoma japonicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6
-
GSH selenoenzyme Schistosoma japonicum
16.6
-
GSH wild-type enzyme Schistosoma japonicum