Structural highlights
Function
[PRDX3_HUMAN] Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.[1]
Publication Abstract from PubMed
Peroxiredoxins are abundant peroxidase enzymes that are key regulators of the cellular redox environment. A major subgroup of these proteins, the typical 2-Cys peroxiredoxins, can switch between dimers and decameric or dodecameric rings, during the catalytic cycle. The necessity of this change in quaternary structure for function as a peroxidase is not fully understood. In order to explore this, human peroxiredoxin 3 (Prx3) protein was engineered to form both obligate dimers (S75E Prx3) and stabilised dodecameric rings (S78C Prx3), uncoupling structural transformations from the catalytic cycle. The obligate dimer, S75E Prx3, retained catalytic activity towards hydrogen peroxide, albeit significantly lower than the wildtype and S78C proteins, suggesting an evolutionary advantage of having higher order self-assemblies.
Quaternary structure influences the peroxidase activity of peroxiredoxin 3.,Yewdall NA, Peskin AV, Hampton MB, Goldstone DC, Pearce FG, Gerrard JA Biochem Biophys Res Commun. 2018 Feb 10. pii: S0006-291X(18)30322-X. doi:, 10.1016/j.bbrc.2018.02.093. PMID:29438714[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T. Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically. Eur J Biochem. 2003 Jan;270(1):76-83. PMID:12492477
- ↑ Yewdall NA, Peskin AV, Hampton MB, Goldstone DC, Pearce FG, Gerrard JA. Quaternary structure influences the peroxidase activity of peroxiredoxin 3. Biochem Biophys Res Commun. 2018 Feb 10. pii: S0006-291X(18)30322-X. doi:, 10.1016/j.bbrc.2018.02.093. PMID:29438714 doi:http://dx.doi.org/10.1016/j.bbrc.2018.02.093
