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

BRENDA support

Literature summary for 1.8.98.2 extracted from

  • Findlay, V.J.; Tapiero, H.; Townsend, D.M.
    Sulfiredoxin: a potential therapeutic agent? (2005), Biomed. Pharmacother., 59, 374-379.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH Homo sapiens antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
?