Reactome | PRDX1 overoxidizes

PRDX1 overoxidizes

Stable Identifier

R-HSA-5631885

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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        NFE2L2 regulating anti-oxidant/detoxification enzymes (Homo sapiens)
        
        PRDX1 overoxidizes (Homo sapiens)

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The activity of eukaryotic PRDX1 gradually decreases with time, which is due to the overoxidation of the catalytic cysteine C52. Normally, oxidized cysteine C52-SOH is generated as a catalytic intermediate, which is subsequently reduced by thioredoxin. Occasionally, further oxidation happens, generating C52-SOOH , where the catalytic cysteine is converted to cysteine-sulfinic acid. This over-oxidation cannot be reversed by thioredoxin (Yang et al. 2002, Budanov et al. 2004). Bacterial peroxiredoxin AhpC does not undergo over-oxidation due to structural difference (Wood et al. 2003).

Literature References

PubMed ID	Title	Journal	Year
12161445	Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid Yang, KS, Kang, SW, Woo, HA, Hwang, SC, Chae, HZ, Kim, K, Rhee, SG	J. Biol. Chem.	2002
12714747	Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Wood, ZA, Poole, LB, Karplus, PA	Science	2003
15105503	Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD Budanov, AV, Sablina, AA, Feinstein, E, Koonin, EV, Chumakov, PM	Science	2004