PRDX1 overoxidizes

Stable Identifier
Reaction [transition]
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

Woo, HA, Kim, K, Yang, KS, Kang, SW, Chae, HZ, Hwang, SC, 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

Feinstein, E, Budanov, AV, Chumakov, PM, Koonin, EV, Sablina, AA

Science 2004
Catalyst Activity

peroxidase activity of PRDX1 dimer [cytosol]

Orthologous Events
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