Peroxiredoxin
FunctionPeroxiredoxin (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
Atypical 2-Cys Prx
1-Cys Prx
RelevancePrx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8]. Structural highlightsIn the typical 2-cysteine Prx the Cys-Cys bond is formed between two subunits[9]. Cl coordination site.
| ||||||||||||
3D Structures of Peroxiredoxin
Updated on 29-May-2019
- Peroxiredoxin
- 1qq2 – r2Cys-Prx – rat
- 2c0d – Pf2Cys-Prx – Plasmodium falciparum
- 1xiy – Pf1Cys-Prx
- 1xcc, 2h01, 3tb2 - 1Cys-Prx – Plasmodium yoelii
- 2i81 - 2Cys-Prx – Plasmodium vivax
- 1qmv - h2Cys-Prx – human
- 2a4v – yPrx dot5 C-terminal (mutant) – yeast
- 3cmi – yPrx hyr1 - yeast
- 5ept - yPrx tsa2
- 3sbc – yPrx tsa1 (mutant)
- 5dvb - yPrx tsa2 (mutant)
- 4g2e – Prx – Sulfolobus tokodaii
- 6q5v – Prx – Sulfolobus islandicus
- 5xbr – PhPrx – Pyrococcus horikoshii
- 5xbq – PhPrx (mutant)
- 4llr - 2Cys-Prx – Trypanosoma cruzi
- 1we0 – Prx – Amphibacillus xylanus
- 2cv4, 2cx3, 2cx4 – ApPrx – Aeropyrum pernix
- 5xbs – ApPrx (mutant)
- 3drn – SsPrx – Sulfolobus solfataricus
- 3hjp – SsPrx (mutant)
- 3ixr – Prx PRXQ (mutant) – Xylella fastidiosa
- 5epf - Prx – Mycobacterium tuberculosis
- 1qq2 – r2Cys-Prx – rat
- Peroxiredoxin 1
- Peroxiredoxin 2
- Peroxiredoxin 3
- Peroxiredoxin 4
- Peroxiredoxin 5
- Peroxiredoxin 6
- Peroxiredoxin Asp F3