This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Peroxiredoxin
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_1qq2| PDB=1qq2 | SIZE=400| SCENE= |right|CAPTION= | + | {{STRUCTURE_1qq2| PDB=1qq2 | SIZE=400| SCENE= |right|CAPTION=Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]}} |
== Function == | == Function == | ||
[[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. | [[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. | ||
| Line 15: | Line 15: | ||
== Relevance == | == Relevance == | ||
Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | ||
| + | |||
| + | == Structural highlights == | ||
| + | In the typical 2-cysteine Prx the Cys-Cys bond is formed between two subunits<ref>PMID:10535922</ref>. | ||
== 3D Structures of Peroxiredoxin == | == 3D Structures of Peroxiredoxin == | ||
Revision as of 07:56, 22 June 2016
Contents |
Function
Peroxiredoxin (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: typical 2-Cysteine Prx in which the Cys-Cys bond is formed between two subunits, atypical 2-Cys Prx in which the bond is formed within one subunit and 1-Cysteine Prx which uses a single Cys residue for the catalysis.
Typical 2-Cys Prx
- Prx 1 interacts with signaling molecules[1].
- Prx 2 is essential for sustaining erythrocyte life span[2].
- Prx 3 is mitochondria-specific.[3].
- Prx 4 localizes to the cytoplasm and regulates the activation of NF-κB[4].
Atypical 2-Cys Prx
- Prx 5 protects from mitochondrial DNA damage induced by H2O2[5].
1-Cys Prx
- Prx 6 reduces peroxidized membrane phospholipids[6].
Relevance
Prx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8].
Structural highlights
In the typical 2-cysteine Prx the Cys-Cys bond is formed between two subunits[9].
3D Structures of Peroxiredoxin
Updated on 22-June-2016
References
- ↑ Neumann CA, Cao J, Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle. 2009 Dec 15;8(24):4072-8. Epub 2009 Dec 5. PMID:19923889 doi:http://dx.doi.org/10.4161/cc.8.24.10242
- ↑ Low FM, Hampton MB, Winterbourn CC. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid Redox Signal. 2008 Sep;10(9):1621-30. doi: 10.1089/ars.2008.2081. PMID:18479207 doi:http://dx.doi.org/10.1089/ars.2008.2081
- ↑ Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J Biol Chem. 2004 Oct 1;279(40):41975-84. Epub 2004 Jul 27. PMID:15280382 doi:http://dx.doi.org/10.1074/jbc.M407707200
- ↑ Fujii J, Ikeda Y, Kurahashi T, Homma T. Physiological and pathological views of peroxiredoxin 4. Free Radic Biol Med. 2015 Jun;83:373-9. doi: 10.1016/j.freeradbiomed.2015.01.025., Epub 2015 Feb 2. PMID:25656995 doi:http://dx.doi.org/10.1016/j.freeradbiomed.2015.01.025
- ↑ Banmeyer I, Marchand C, Clippe A, Knoops B. Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide. FEBS Lett. 2005 Apr 25;579(11):2327-33. PMID:15848167 doi:http://dx.doi.org/10.1016/j.febslet.2005.03.027
- ↑ Fisher AB. Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A(2) activities. Antioxid Redox Signal. 2011 Aug 1;15(3):831-44. doi: 10.1089/ars.2010.3412. Epub , 2011 Mar 31. PMID:20919932 doi:http://dx.doi.org/10.1089/ars.2010.3412
- ↑ Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ. Overexpression of peroxiredoxin in human breast cancer. Anticancer Res. 2001 May-Jun;21(3B):2085-90. PMID:11497302
- ↑ Rafiei S, Tiedemann K, Tabaries S, Siegel PM, Komarova SV. Peroxiredoxin 4: a novel secreted mediator of cancer induced osteoclastogenesis. Cancer Lett. 2015 Jun 1;361(2):262-70. doi: 10.1016/j.canlet.2015.03.012. Epub, 2015 Mar 14. PMID:25779674 doi:http://dx.doi.org/10.1016/j.canlet.2015.03.012
- ↑ Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12333-8. PMID:10535922
