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RESEARCH PRODUCT

Structure, mechanism and regulation of peroxiredoxins.

J. Robin HarrisZachary A. WoodLeslie B. PooleEwald Schröder

subject

Peroxiredoxin-4Binding SitesChemistryProtein ConformationPeroxiredoxin IIIPeroxiredoxin 2PeroxiredoxinsBiochemistryCatalysischemistry.chemical_compoundSulfiredoxinCatalytic cycleBiochemistryPeroxidasesSulfenic acidPeroxiredoxinMolecular BiologyDimerizationOxidation-ReductionCysteine

description

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.

yearjournalcountryeditionlanguage
2003-01-09Trends in biochemical sciences
10.1016/s0968-0004(02)00003-8https://pubmed.ncbi.nlm.nih.gov/12517450