IPR000866
Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant
InterPro entry
Short name | AhpC/TSA |
Overlapping homologous superfamilies | |
domain relationships |
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 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 (the peroxidatic 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. 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
[1].
Alkyl hydroperoxide reductase (Ahp) has two subunits, the small AhpC subunit and the large AhpF subunit
[2]. AhpC is responsible for directly reducing organic hydroperoxides in its reduced dithiol form. Thiol specific antioxidant (TSA) is a physiologically important antioxidant which constitutes an enzymatic defence against sulphur-containing radicals and protects the cell against the oxidative stress caused by protein misfolding and aggregation
[3]. This entry contains AhpC and TSA, as well as related proteins.
References
1.Structure, mechanism and regulation of peroxiredoxins. Wood ZA, Schroder E, Robin Harris J, Poole LB. Trends Biochem. Sci. 28, 32-40, (2003). View articlePMID: 12517450
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- Pfam:PF00578
Representative structure
5c04: Crystal structure of the F37H mutant AhpE from Mycobacterium tuberculosis