Reactome | SRXN1 reduces hyperoxidized PRDX1 dimer

SRXN1 reduces hyperoxidized PRDX1 dimer

Stable Identifier

R-HSA-9760094

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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Cellular responses to stimuli (Homo sapiens)

- Cellular responses to stress (Homo sapiens)
  - Cellular response to chemical stress (Homo sapiens)
    - KEAP1-NFE2L2 pathway (Homo sapiens)
      - Nuclear events mediated by NFE2L2 (Homo sapiens)
        
        NFE2L2 regulating anti-oxidant/detoxification enzymes (Homo sapiens)
        
        SRXN1 reduces hyperoxidized PRDX1 dimer (Homo sapiens)

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SRXN1 is a sulfiredoxin protein that reduces hyperoxidized members of the PRDX family in response to H2O2. PRDX dimers respond to the oxidative challenge of intracellular H2O2 through the two-step formation of an internal disulphide bond during the process of H2O2 reduction. This disulphide bond can be reduced by thioredoxin (TRX), regenerating the catalytically active PRDX dimer.

In some instances, the second step in this pathway is replaced by the hyperoxidation of the PRDX dimer to sulfinic acid, which is not reduceable by TRX. While this was previously thought to be irreversible, SRXN1 has been shown to reduce sulfinic acid in some PRDX family members, restoring the enzymatic activity (Chang et al, 2004; Woo et al, 2005).

Literature References

PubMed ID	Title	Journal	Year
15590625	Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins Yang, JS, Woo, HA, Park, SJ, Chang, TS, Jeong, W, Park, KJ, Rhee, SG	J Biol Chem	2005
15448164	Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine Woo, HA, Lee, SM, Chang, TS, Jeong, W, Park, S, Rhee, SG	J Biol Chem	2004