PRDX6

From Wikipedia, the free encyclopedia

Peroxiredoxin 6

PDB rendering based on 1prx.

Available structures: 1prx

Identifiers

Symbol(s)

PRDX6; 1-Cys; AOP2; KIAA0106; MGC46173; NSGPx; PRX; aiPLA2; p29

External IDs

OMIM: 602316 MGI: 894320 HomoloGene: 3606

Gene ontology
Molecular Function:	• phospholipase A2 activity • oxidoreductase activity • hydrolase activity • peroxiredoxin activity
Cellular Component:	• lysosome • cytosol
Biological Process:	• response to oxidative stress • phospholipid catabolic process • lipid catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004905 (mRNA)
NP_004896 (protein)

XM_001000157 (mRNA)
XP_001000157 (protein)

Location

Chr 1: 171.71 - 171.72 Mb

Chr 1: 163.08 - 163.09 Mb

Pubmed search

[1]

[2]

Peroxiredoxin 6, also known as PRDX6, is a human gene.^[1]

The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRDX6 peroxiredoxin 6.

[edit] Further reading

Phelan SA (2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant.". Antioxid. Redox Signal. 1 (4): 571-84. PMID 11233154.
Manevich Y, Fisher AB (2005). "Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism.". Free Radic. Biol. Med. 38 (11): 1422-32. doi:10.1016/j.freeradbiomed.2005.02.011. PMID 15890616.
Akesson B (1975). "Work in progress. Occurrence of phospholipase A1 and A2 in human decidua.". Prostaglandins 9 (5): 667-73. PMID 240188.
Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison.". Electrophoresis 13 (12): 992-1001. PMID 1286669.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317-20. PMID 1602151.
Yeats DA, Bakhle YS (1989). "Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity.". Biochim. Biophys. Acta 1003 (2): 189-95. PMID 2730891.
Nagase T, Miyajima N, Tanaka A, et al. (1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (1): 37-43. PMID 7788527.
Golaz O, Hughes GJ, Frutiger S, et al. (1994). "Plasma and red blood cell protein maps: update 1993.". Electrophoresis 14 (11): 1223-31. PMID 8313871.
Kim TS, Sundaresh CS, Feinstein SI, et al. (1997). "Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein.". J. Biol. Chem. 272 (4): 2542-50. PMID 8999971.
Frank S, Munz B, Werner S (1997). "The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene.". Oncogene 14 (8): 915-21. doi:10.1038/sj.onc.1200905. PMID 9050990.
Kang SW, Baines IC, Rhee SG (1998). "Characterization of a mammalian peroxiredoxin that contains one conserved cysteine.". J. Biol. Chem. 273 (11): 6303-11. PMID 9497358.
Choi HJ, Kang SW, Yang CH, et al. (1998). "Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.". Nat. Struct. Biol. 5 (5): 400-6. PMID 9587003.
Chen JW, Dodia C, Feinstein SI, et al. (2000). "1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities.". J. Biol. Chem. 275 (37): 28421-7. doi:10.1074/jbc.M005073200. PMID 10893423.
Fatma N, Singh DP, Shinohara T, Chylack LT (2002). "Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress.". J. Biol. Chem. 276 (52): 48899-907. doi:10.1074/jbc.M100733200. PMID 11677226.
Wagner E, Luche S, Penna L, et al. (2002). "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress.". Biochem. J. 366 (Pt 3): 777-85. doi:10.1042/BJ20020525. PMID 12059788.
Leavey PJ, Gonzalez-Aller C, Thurman G, et al. (2003). "A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity.". J. Biol. Chem. 277 (47): 45181-7. doi:10.1074/jbc.M202869200. PMID 12121978.
Manevich Y, Sweitzer T, Pak JH, et al. (2002). "1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage.". Proc. Natl. Acad. Sci. U.S.A. 99 (18): 11599-604. doi:10.1073/pnas.182384499. PMID 12193653.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Krapfenbauer K, Engidawork E, Cairns N, et al. (2003). "Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders.". Brain Res. 967 (1-2): 152-60. PMID 12650976.