title: Structure, mechanism and regulation of peroxiredoxins.
abstract: Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerization states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidized to a sulfenic acid by the peroxide substrate. The recycling of the sulfenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity.
authors.affiliation: Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403, USA.
authors.forename: Zachary A
authors.initials: ZA
authors.lastname: Wood
authors.forename: Ewald
authors.initials: E
authors.lastname: Schröder
authors.forename: J
authors.initials: J
authors.lastname: Robin Harris
authors.forename: Leslie B
authors.initials: LB
authors.lastname: Poole
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D019281:Dimerization; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D054464:Peroxiredoxins; D011487:Protein Conformation
chemical_list: D010544:Peroxidases; D054464:Peroxiredoxins