Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.24 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

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

Inhibitors

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

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
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

Cofactor Comment Organism Structure
thioredoxin
-
Saccharomyces cerevisiae