PRDX1 overoxidizes

Stable Identifier
R-HSA-5631885
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
12714747 Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

Wood, ZA, Poole, LB, Karplus, PA

Science 2003
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
15105503 Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

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

Science 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
peroxidase activity of PRDX1 dimer [cytosol]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created