PRDX6

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1PRX, 5B6N, 5B6M

Identifiers

Aliases

PRDX6, 1-Cys, AOP2, HEL-S-128m, NSGPx, PRX, aiPLA2, p29, peroxiredoxin 6

External IDs

MGI: 894320 HomoloGene: 3606 GeneCards: PRDX6

EC number

1.11.1.9

Gene ontology
Molecular function	• peroxidase activity • glutathione peroxidase activity • catalytic activity • protein binding • peroxiredoxin activity • oxidoreductase activity • hydrolase activity • ubiquitin protein ligase binding • cadherin binding involved in cell-cell adhesion • antioxidant activity
Cellular component	• cytoplasm • cytosol • membrane • cytoplasmic, membrane-bounded vesicle • extracellular fluid • lysosome • extracellular exosome • cytoplasmic vesicle • cell-cell adherens junction
Biological process	• lipid metabolic process • response to reactive oxygen species • lipid catabolic process • hydrogen peroxide catabolic process • metabolic process • oxidation-reduction process • cellular oxidant detoxification • cell-cell adhesion • cell redox homeostasis
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


9588


11758

Ensembl


ENSG00000117592


ENSMUSG00000026701

UniProt


P30041


O08709

RefSeq (mRNA)


NM_004905


NM_001303408 NM_007453

RefSeq (protein)


NP_004896.1


NP_031479.1

Location (UCSC)

Chr 1: 173.48 – 173.49 Mb

Chr 1: 161.24 – 161.25 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene.^[3]^[4] It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

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.^[4]

Model organisms

*Prdx6* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Tail epidermis wholemount	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Salmonella infection	Normal^[5]
Citrobacter infection	Normal^[6]
All tests and analysis from^[7]^[8]

Model organisms have been used in the study of PRDX6 function. A conditional knockout mouse line, called Prdx6^{tm1a(EUCOMM)Wtsi}^[9]^[10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.^[11]^[12]^[13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[7]^[14] Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.^[7]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Phelan SA (Mar 2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant". Antioxid Redox Signal. 1 (4): 571–84. PMID 11233154.
1 2 "Entrez Gene: PRDX6 peroxiredoxin 6".
↑ "Salmonella infection data for Prdx6". Wellcome Trust Sanger Institute.
↑ "Citrobacter infection data for Prdx6". Wellcome Trust Sanger Institute.
1 2 3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
↑ "International Knockout Mouse Consortium".
↑ "Mouse Genome Informatics".
↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
↑ Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

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; Gustavii, B (1975). "Work in progress. Occurrence of phospholipase A1 and A2 in human decidua". Prostaglandins. 9 (5): 667–73. doi:10.1016/0090-6980(75)90106-9. 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. doi:10.1002/elps.11501301201. PMID 1286669.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. 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. doi:10.1016/0005-2760(89)90254-3. 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. doi:10.1093/dnares/2.1.37. 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. doi:10.1002/elps.11501401183. 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. doi:10.1074/jbc.272.4.2542. 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. doi:10.1074/jbc.273.11.6303. 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. doi:10.1038/nsb0598-400. 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. PMC 1222825. 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. PMC 129315. 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. PMC 139241. 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. doi:10.1016/S0006-8993(02)04243-9. PMID 12650976.

PDB gallery

1prx: HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Oxidoreductases: peroxidases (EC 1.11)

1.11.1.1-14	Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 2 3 4 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase

1.11.1.15 (peroxiredoxin)	1 2 3 4 5 6

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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PRDX6

Function

Model organisms

References

Further reading