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Literature summary for 1.11.1.9 extracted from

  • Ren, X.; Jemth, P.; Board, P.G.; Luo, G.; Mannervik, B.; Liu, J.; Zhang, K.; Shen, J.
    A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase (2002), Chem. Biol., 9, 789-794.
    View publication on PubMed

Application

Application Comment Organism
medicine the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology. Rat theta-class glutathione transferase T2-2 (rGST T2-2) presents an ideal scaffold for the design of a novel glutathione peroxidase catalyst because it binds GSH and contains a serine close to substrate binding site, which can be chemically modified to bind selenium. The modified Se-rGST T2-2 efficiently catalyzes the reduction of hydrogen peroxide, and the glutathione peroxidase activity surpasses the activities of some natural glutathione peroxidases Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2O2 + GSH Rattus norvegicus the enzyme protects cells against oxidative damage H2O + GSSG
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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rat theta-class glutathione transferase T2-2 (rGST T2-2) presents an ideal scaffold for the design of a novel glutathione peroxidase catalyst because it binds GSH and contains a serine close to substrate binding site, which can be chemically modified to bind selenium. The modified Se-rGST T2-2 efficiently catalyzes the reduction of hydrogen peroxide, and the glutathione peroxidase activity surpasses the activities of some natural glutathione peroxidases
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 + GSH the enzyme protects cells against oxidative damage Rattus norvegicus H2O + GSSG
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?

Synonyms

Synonyms Comment Organism
GPX
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Rattus norvegicus