PTHR10430

PEROXIREDOXIN

PANTHER entry
Member databasePANTHER
PANTHER typefamily

Description
Imported from IPR037944

PRX5-like proteins belongs to the peroxiredoxin (PRX) family
[1]
. PRX5 is a homodimeric thioredoxin (TRX) peroxidase widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol
[3]
. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction
[2]
. Budding yeast PRX5 homologue, Ahp1, may act as both a peroxidase and a receptor for alkylhydroperoxides
[4]
. Pmp20 from fission yeast may act as a chaperone rather than a peroxidase
[5]
.

As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs
[7, 6]
.

References
Imported from IPR037944

1.Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor. Copley SD, Novak WR, Babbitt PC. Biochemistry 43, 13981-95, (2004). View articlePMID: 15518547

2.Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice. Plaisant F, Clippe A, Vander Stricht D, Knoops B, Gressens P. Free Radic. Biol. Med. 34, 862-72, (2003). View articlePMID: 12654475

3.Human peroxiredoxin 5 is a peroxynitrite reductase. Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, Kissner R, Koppenol WH, Rees JF, Knoops B. FEBS Lett. 571, 161-5, (2004). View articlePMID: 15280035

4.Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to induce disulfide bond formation in the Cad1 transcription factor. Iwai K, Naganuma A, Kuge S. J. Biol. Chem. 285, 10597-604, (2010). View articlePMID: 20145245

5.Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe. Kim JS, Bang MA, Lee S, Chae HZ, Kim K. BMB Rep 43, 170-5, (2010). View articlePMID: 20356456

6.Structure, mechanism and regulation of peroxiredoxins. Wood ZA, Schroder E, Robin Harris J, Poole LB. Trends Biochem. Sci. 28, 32-40, (2003). View articlePMID: 12517450

7.Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP. J. Mol. Biol. 337, 1079-90, (2004). View articlePMID: 15046979

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