title: Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.
abstract: Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H(2)O(2). Mammalian cells express six Prx isoforms that are localized to various cellular compartments. The oxidized active site cysteine of Prx can be reduced by a cellular thiol, thus enabling Prx to function as a locally constrained peroxidase. Regulation of Prx via phosphorylation in response to extracellular signals allows the local accumulation of H(2)O(2) and thereby enables its messenger function. The fact that the oxidation state of the active site cysteine of Prx can be transferred to other proteins that are less intrinsically susceptible to H(2)O(2) also allows Prx to function as an H(2)O(2) sensor.
authors.affiliation: Division of Life and Pharmaceutical Sciences, Ewha Womans University,Seoul 120-750, Korea. rheesg@ewha.ac.kr
authors.forename: Sue Goo
authors.initials: SG
authors.lastname: Rhee
authors.forename: Hyun Ae
authors.initials: HA
authors.lastname: Woo
authors.forename: In Sup
authors.initials: IS
authors.lastname: Kil
authors.forename: Soo Han
authors.initials: SH
authors.lastname: Bae
mesh_terms: D000818:Animals; D020134:Catalytic Domain / Q000502:physiology; D003545:Cysteine / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D054464:Peroxiredoxins / Q000378:metabolism*; D010766:Phosphorylation / Q000502:physiology; D015290:Second Messenger Systems / Q000502:physiology*
chemical_list: D007527:Isoenzymes; D006861:Hydrogen Peroxide; D054464:Peroxiredoxins; D009195:Peroxidase; D003545:Cysteine