Structure, mechanism and regulation of peroxiredoxins

Trends Biochem Sci. 2003 Jan;28(1):32-40. doi: 10.1016/s0968-0004(02)00003-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Binding Sites
  • Catalysis
  • Dimerization
  • Oxidation-Reduction
  • Peroxidases / chemistry
  • Peroxidases / metabolism*
  • Peroxiredoxins
  • Protein Conformation

Substances

  • Peroxidases
  • Peroxiredoxins