Literature summary for 1.11.1.24 extracted from

Ikeda, Y.; Nakano, M.; Ihara, H.; Ito, R.; Taniguchi, N.; Fujii, J.
Different consequences of reactions with hydrogen peroxide and t-butyl hydroperoxide in the hyperoxidative inactivation of rat peroxiredoxin-4 (2011), J. Biochem., 149, 443-453.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
C126S	very weak activity both with substrate H2O2 and t-butyl hydroperoxide	Rattus norvegicus
C150S	activity similar to wild-type	Rattus norvegicus
C247S	weak activity both with substrate H2O2 and t-butyl hydroperoxide	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Rattus norvegicus	5783	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q9Z0V5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme is inactivated by hyperoxidation of the peroxidatic cysteine to a sulfinic acid in a catalytic cycle-dependent manner. The peroxidase activity of isoform Prx-4 is almost completely inhibited in the reaction with t-butyl hydroperoxide. When H2O2 is used as the substrate, the peroxidase activity significantly remains after oxidative damage. Both reactions result in the same oxidative damage, i.e. sulfinic acid formation at the peroxidatic cysteine	Rattus norvegicus	?	-	?

Synonyms

Synonyms	Comment	Organism
peroxiredoxin-4	-	Rattus norvegicus
Prx-4	-	Rattus norvegicus

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Release 2023.1 (January 2023)