Literature summary for 1.8.98.2 extracted from

Moon, J.C.; Kim, G.M.; Kim, E.K.; Lee, H.N.; Ha, B.; Lee, S.Y.; Jang, H.H.
Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin (2013), Biochem. Biophys. Res. Commun., 432, 291-295.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C84S	Srx1 reactivates the yeast Prx1 peroxidase activity that is inactivated by H2O2. Mutant C84S does not induce the reactivation of inactivated Prx1 or dissociation of the high molecular weight Prx1 complex	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Synonyms

Synonyms	Comment	Organism
Srx1	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
physiological function	sulfiredoxin Srx1 reactivates the yeast peroxiredoxin Prx1 peroxidase activity that is inactivated by H2O2, whereas it decreases the chaperone activity enhanced by H2O2. Srx1 dissociates the H2O2-induced high molecular weight Prx1 complex, and the Srx1 Cys84 residue is critical for its dissociation	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)