PRDX5

PRDX5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRDX5, ACR1, AOEB166, B166, HEL-S-55, PLP, PMP20, PRDX6, PRXV, prx-V, SBBI10, peroxiredoxin 5
External IDsOMIM: 606583; MGI: 1859821; HomoloGene: 8076; GeneCards: PRDX5; OMA:PRDX5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012094
NM_181651
NM_181652
NM_001358511
NM_001358516

NM_012021
NM_001358444

RefSeq (protein)

NP_036226
NP_857634
NP_857635
NP_001345440
NP_001345445

NP_036151
NP_001345373

Location (UCSC)Chr 11: 64.32 – 64.32 MbChr 19: 6.88 – 6.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Peroxiredoxin-5 (PRDX5), mitochondrial is a protein that in humans is encoded by the PRDX5 gene, located on chromosome 11.[5]

This gene encodes a member of the six-member peroxiredoxin family of antioxidant enzymes. Like the other five members, PRDX5 is widely expressed in tissues but differs by its large subcellular distribution.[6] In human cells, it has been shown that PRDX5 can be localized to mitochondria, peroxisomes, the cytosol, and the nucleus.[7] Human PRDX5 is identified by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20.[6][8]

Biochemically, PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce alkyl hydroperoxides or peroxynitrite with high rate constants in the 106 to 107 M−1s−1 range, whereas its reaction with hydrogen peroxide is more modest, in the 105 M−1s−1 range.[7] So far, PRDX5 has been shown to be a cytoprotective antioxidant enzyme that inhibits endogenous or exogenous peroxide accumulation.[7]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000126432Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024953Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "PRDX5 peroxiredoxin 5 [Homo sapiens (human)]". NCBI. Retrieved 2016-07-19.
  6. ^ a b Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY (February 2000). "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis". Biochemical and Biophysical Research Communications. 268 (3): 921–7. doi:10.1006/bbrc.2000.2231. PMID 10679306.
  7. ^ a b c Knoops B, Goemaere J, Van der Eecken V, Declercq JP (August 2011). "Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin". Antioxidants & Redox Signaling. 15 (3): 817–29. doi:10.1089/ars.2010.3584. PMID 20977338.
  8. ^ Yamashita H, Avraham S, Jiang S, London R, Van Veldhoven PP, Subramani S, Rogers RA, Avraham H (October 1999). "Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro". The Journal of Biological Chemistry. 274 (42): 29897–904. doi:10.1074/jbc.274.42.29897. PMID 10514471.