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 oligomerisation 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 is oxidised to a sulphenic acid by the peroxide substrate. The recycling of the sulphenic acid back to a thiol is what distinguishes the three enzyme classes .
Wheat peroxiredoxin was detected as a minor allergen binding IgE predominantly from patients with baker's asthma .
Family-defining Pfam domains (at least one of these domains is present in each family member):
|Pfam domain||Pfam clan|
|PF10417||C-terminal domain of 1-Cys peroxiredoxin||-|
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