Peroxiredoxin

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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.
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'''Typical 2-Cys Prx'''<br />
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* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 2''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 3''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 4''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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'''Atypical 2-Cys Prx'''<br />
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* '''Prx 5''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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'''1-Cys Prx'''<br />
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* '''Prx 6''' interacts with signaling molecules<ref>PMID:19923889</ref>.
== Relevance ==
== Relevance ==

Revision as of 10:24, 21 June 2016

Template:STRUCTURE 1qq2

Contents

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

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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