Peroxiredoxin: Difference between revisions
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== Function == | == Function == | ||
[[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide. The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. Prx 5 is expressed in mammalian tissue. | [[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide. The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. Prx 5 is expressed in mammalian tissue. | ||
'''Typical 2-Cys Prx'''<br /> | |||
* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
* '''Prx 2''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
* '''Prx 3''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
* '''Prx 4''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
'''Atypical 2-Cys Prx'''<br /> | |||
* '''Prx 5''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
'''1-Cys Prx'''<br /> | |||
* '''Prx 6''' interacts with signaling molecules<ref>PMID:19923889</ref>. | |||
== Relevance == | == Relevance == | ||
Revision as of 10:24, 21 June 2016
Function
Peroxiredoxin (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide. The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. Prx 5 is expressed in mammalian tissue.
Typical 2-Cys Prx
- Prx 1 interacts with signaling molecules[1].
- Prx 2 interacts with signaling molecules[2].
- Prx 3 interacts with signaling molecules[3].
- Prx 4 interacts with signaling molecules[4].
Atypical 2-Cys Prx
- Prx 5 interacts with signaling molecules[5].
1-Cys Prx
- Prx 6 interacts with signaling molecules[6].
Relevance
Prx are over expressed in cancer tissue[7].
3D Structures of Peroxiredoxin
Updated on 21-June-2016
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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