Literature summary for 1.11.1.27 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 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bos taurus

Source Tissue

Source Tissue	Comment	Organism	Textmining
lung	-	Bos taurus	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
1-Cys peroxiredoxin	-	Bos taurus
1-CysPrx	-	Bos taurus

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Release 2023.1 (January 2023)