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).
Woo, HA, Kim, K, Yang, KS, Kang, SW, Chae, HZ, Hwang, SC, Rhee, SG
Wood, ZA, Poole, LB, Karplus, PA
Feinstein, E, Budanov, AV, Chumakov, PM, Koonin, EV, Sablina, AA
peroxidase activity of PRDX1 dimer [cytosol]
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