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Literature summary for 1.8.1.9 extracted from

  • Greetham, D.; Grant, C.M.
    Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo (2009), Mol. Cell. Biol., 29, 3229-3240.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thioredoxin disulfide + NADPH + H+ Saccharomyces cerevisiae
-
thioredoxin + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA His Bind resin column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thioredoxin disulfide + NADPH + H+
-
Saccharomyces cerevisiae thioredoxin + NADP+
-
?

Synonyms

Synonyms Comment Organism
thioredoxin reductase
-
Saccharomyces cerevisiae
TRR2
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function Trr2/Trx3 and Trr2/GSH systems exhibit similar capacities for supporting peroxidredoxin 1 catalysis. TRR2 is required for cadmium and hydrogen peroxide resistance promoted by overexpression of peroxiredoxin 1 Saccharomyces cerevisiae