Structure, mechanism and regulation of peroxiredoxins, Trends Biochem：（学生物化学结构、机制和调节抗氧化蛋白的趋势）.pdfVIP

32 Review TRENDS in Biochemical Sciences Vol.28 No.1 January 2003 Structure, mechanism and regulation of peroxiredoxins 1 2 3 2 Zachary A. Wood , Ewald Schro¨ der , J. Robin Harris and Leslie B. Poole 1Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403, USA 2Department of Biochemistry, Wake Forest (University School of Medicine, Winston-Salem, NC 27157, USA 3Institute of Zoology, University of Mainz, D-55099 Mainz, Germany Peroxiredoxins (Prxs) are a ubiquitous family of antioxi- functions of Prxs probably overlap to some extent with dant enzymes that also control cytokine-induced per- those of the better known glutathione peroxidases and oxide levels which mediate signal transduction in catalases, although it has been suggested that their mammalian cells. Prxs can be regulated by changes to moderate catalytic efficiencies (, 105 M 21 s21) compared phosphorylation, redox and possibly oligomerization with those of glutathione peroxidases (, 108 M 21 s21) [3] states. Prxs are divided into three classes: typical 2-Cys and catalases (, 106 M 21 s21) [14] makes their importance Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share as peroxidases questionable [3]. Nonetheless, the high the same basic catalytic mechanism, in which an active- abundance of Prxs in a wide range of cells and a recent site cysteine (the peroxidatic cysteine) is oxidized to a finding that a bacterial Prx [alkyl hydroperoxide reductase sulfenic acid by the peroxide substrate. The recycling of C22 (AhpC)] and not catalase i