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Literature summary extracted from

  • Manevich, Y.; Feinstein, S.I.; Fisher, A.B.
    Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST (2004), Proc. Natl. Acad. Sci. USA, 101, 3780-3785 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.11.1.27 additional information physiological mechanism for the glutathionylation of the oxidized cysteine in 1-cysPrx by its heterodimerization with glutathione-loaded glutathione S-transferase P (GST-pi) results in heterodimer formation, glutathionylation of the enzyme (1-cysPrx), and enzyme reactivation. Maximum activation of the enzyme (1-cysPrx) occurrs with a 1:1 molar ratio of glutathione-saturated glutathione S-transferase P and a 2:1 molar ratio of glutathione to enzyme (1-cysPrx) Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.27 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.27
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.27 lung
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.27 2 glutathione + 1-palmitoyl-2-linolenoyl hydroperoxide-sn-glycero-3-phosphocholine
-
 Bos taurus glutathione disulfide + H2O + ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.27 1-Cys peroxiredoxin
-
 Bos taurus
1.11.1.27 1-CysPrx
-
 Bos taurus