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Literature summary extracted from

  • Trotter, E.W.; Rand, J.D.; Vickerstaff, J.; Grant, C.M.
    The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant (2008), Biochem. J., 412, 73-80.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.24 C47S the Cys47 residue of Tsa1 is not required for chaperone activity but is essential for peroxidase activity Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.24 additional information insensitive to hygromycin, paromomycin, and cycloheximide Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.24 ribosome
-
 Saccharomyces cerevisiae 5840
-

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 H2O2 + reduced thioredoxin
-
 Saccharomyces cerevisiae H2O + oxidized thioredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 Tsa1 has dual activities as a peroxidase and as a molecular chaperone, Tsa1 functions predominantly as an antioxidant in protecting both the cytosol and actively translating ribosomes against endogenous reactive oxygen species, but shifts towards its chaperone function in response to oxidative stress conditions Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
 Saccharomyces cerevisiae