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Peroxisome
A peroxisome (IPA: [pɛɜˈɹɒksɪˌsoʊm])[1] is a type of organelle
known as a microbody, found in virtually all eukaryotic cells.[2]
They are involved in catabolism of very long chain fatty acids,
branched chain fatty acids, D-amino acids, and polyamines,
reduction of reactive oxygen species – specifically hydrogen
peroxide[3] – and biosynthesis of plasmalogens, i.e., ether
phospholipids critical for the normal function of mammalian
brains and lungs.[4] They also contain approximately 10% of the
total activity of two enzymes in the pentose phosphate pathway,
which is important for energy metabolism.[4] It is vigorously
debated whether peroxisomes are involved in isoprenoid and
cholesterol synthesis in animals.[4] Other known peroxisomal
functions include the glyoxylate cycle in germinating seeds
("glyoxysomes"), photorespiration in leaves,[5] glycolysis in
trypanosomes ("glycosomes"), and methanol and/or amine
oxidation and assimilation in some yeasts. Basic structure of a peroxisome

Contents
History
Metabolic functions
Peroxisome assembly
Associated medical conditions
Genes
Evolutionary origins
Other related organelles
See also
References
Further reading
External links

Distribution of peroxisomes (white) in HEK 293

History cells during mitosis

Peroxisomes were identified as organelles by the Belgian

cytologist Christian de Duve in 1967[6] after they had been first described by a Swedish doctoral student, J. Rhodin in
1954.[7]

Metabolic functions
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A major function of the peroxisome is the breakdown of very long chain fatty
acids through beta oxidation. In animal cells, the long fatty acids are converted
to medium chain fatty acids, which are subsequently shuttled to mitochondria
where they are eventually broken down to carbon dioxide and water. In yeast
and plant cells, this process is carried out exclusively in peroxisomes.[8]

The first reactions in the formation of plasmalogen in animal cells also occur in
peroxisomes. Plasmalogen is the most abundant phospholipid in myelin.
Deficiency of plasmalogens causes profound abnormalities in the myelination
of nerve cells, which is one reason why many peroxisomal disorders affect the Peroxisome in rat neonatal
nervous system.[8] Peroxisomes also play a role in the production of bile acids cardiomyocyte
important for the absorption of fats and fat-soluble vitamins, such as vitamins
A and K. Skin disorders are features of genetic disorders affecting peroxisome
function as a result.

Peroxisomes contain oxidative enzymes, such as D-amino acid oxidase and uric acid oxidase.[9] However the last enzyme is
absent in humans, explaining the disease known as gout, caused by the accumulation of uric acid. Certain enzymes within
the peroxisome, by using molecular oxygen, remove hydrogen atoms from specific organic substrates (labeled as R), in an
oxidative reaction, producing hydrogen peroxide (H2O2, itself toxic):

Catalase, another peroxisomal enzyme, uses this H2O2 to oxidize other substrates, including phenols, formic acid,
formaldehyde, and alcohol, by means of the peroxidation reaction:

, thus eliminating the poisonous hydrogen peroxide in the

process.

This reaction is important in liver and kidney cells, where the peroxisomes detoxify various toxic substances that enter the
blood. About 25% of the ethanol alcohol humans drink is oxidized to acetaldehyde in this way.[8] In addition, when excess
H2O2 accumulates in the cell, catalase converts it to H2O through this reaction:

In higher plants, peroxisomes contain also a complex battery of antioxidative enzymes such as superoxide dismutase, the
components of the ascorbate-glutathione cycle, and the NADP-dehydrogenases of the pentose-phosphate pathway. It has
been demonstrated that peroxisomes generate superoxide (O2•−) and nitric oxide (•NO) radicals.[10][11]

The peroxisome of plant cells is polarised when fighting fungal penetration. Infection causes a glucosinolate molecule to
play an antifungal role to be made and delivered to the outside of the cell through the action of the peroxisomal proteins
(PEN2 and PEN3).[12]

Peroxisome assembly
Peroxisomes can be derived from the endoplasmic reticulum and replicate by fission.[13] Peroxisome matrix proteins are
translated in the cytoplasm prior to import. Specific amino acid sequences (PTS or peroxisomal targeting signal) at the C-
terminus (PTS1) or N-terminus (PTS2) of peroxisomal matrix proteins signals them to be imported into the organelle.
There are at least 32 known peroxisomal proteins, called peroxins,[14] which participate in the process of peroxisome
assembly. Proteins do not have to unfold to be imported into the peroxisome. The protein receptors, the peroxins PEX5

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and PEX7, accompany their cargoes (containing a PTS1 or a PTS2 amino acid sequence, respectively) all the way into the
peroxisome where they release the cargo and then return to the cytosol – a step named recycling. A model describing the
import cycle is referred to as the extended shuttle mechanism.[15] There is now evidence that ATP hydrolysis is required
for the recycling of receptors to the cytosol. Also, ubiquitination appears to be crucial for the export of PEX5 from the
peroxisome, to the cytosol.

Associated medical conditions

Peroxisomal disorders are a class of medical conditions that typically affect the human nervous system as well as many
other organ systems. Two common examples are X-linked adrenoleukodystrophy and peroxisome biogenesis
disorders.[16][17]

Genes
PEX genes encode the protein machinery ("peroxins") required for proper peroxisome assembly, as described above.
Membrane assembly and maintenance requires three of these (peroxins 3, 16, and 19) and may occur without the import
of the matrix (lumen) enzymes. Proliferation of the organelle is regulated by Pex11p.

Genes that encode peroxin proteins include: PEX1, PEX2 (PXMP3), PEX3, PEX5, PEX6, PEX7, PEX10, PEX11A, PEX11B,
PEX11G, PEX12, PEX13, PEX14, PEX16, PEX19, PEX26, PEX28, PEX30, and PEX31.

Evolutionary origins
The protein content of peroxisomes varies across species or organism, but the presence of proteins common to many
species has been used to suggest an endosymbiotic origin; that is, peroxisomes evolved from bacteria that invaded larger
cells as parasites, and very gradually evolved a symbiotic relationship.[18] However, this view has been challenged by
recent discoveries.[19] For example, peroxisome-less mutants can restore peroxisomes upon introduction of the wild-type
gene.

Two independent evolutionary analyses of the peroxisomal proteome found homologies between the peroxisomal import
machinery and the ERAD pathway in the endoplasmic reticulum,[20][21] along with a number of metabolic enzymes that
were likely recruited from the mitochondria.[21] Recently, it has been suggested that the peroxisome may have had an
actinobacterial origin,[22] however, this is controversial.[23]

Other related organelles

Other organelles of the microbody family related to peroxisomes include glyoxysomes of plants and filamentous fungi,
glycosomes of kinetoplastids,[24] and Woronin bodies of filamentous fungi.

See also
Peroxisome proliferator-activated receptor

References
1. "Peroxisome" (http://www.merriam-webster.com/dictionary/peroxisome). Online DIctionary. Merriam-Webster.
Retrieved 19 June 2013.

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2. Gabaldón T (Mar 2010). "Peroxisome diversity and evolution" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC281722

9). Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 365 (1541): 765–73.
doi:10.1098/rstb.2009.0240 (https://doi.org/10.1098%2Frstb.2009.0240). PMC 2817229 (https://www.ncbi.nlm.nih.go
v/pmc/articles/PMC2817229). PMID 20124343 (https://www.ncbi.nlm.nih.gov/pubmed/20124343).
3. Bonekamp NA, Völkl A, Fahimi HD, Schrader M (2009). "Reactive oxygen species and peroxisomes: struggling for
balance". BioFactors. 35 (4): 346–55. doi:10.1002/biof.48 (https://doi.org/10.1002%2Fbiof.48). PMID 19459143 (http
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5. Evert RF, Eichhorn SE (2006). Esau's Plant Anatomy: Meristems, Cells, and Tissues of the Plant Body: Their
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6. de Duve C (Apr 1969). "The peroxisome: a new cytoplasmic organelle". Proceedings of the Royal Society of London.
Series B, Biological Sciences. 173 (1030): 71–83. doi:10.1098/rspb.1969.0039 (https://doi.org/10.1098%2Frspb.1969.
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7. Rhodin, J (1954). "Correlation of ultrastructural organization and function in normal and experimentally changed
proximal tubule cells of the mouse kidney". Doctorate Thesis. Karolinska Institutet, Stockholm.
8. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002). "Chapter 12: Peroxisomes". Molecular Biology of
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9. del Río LA, Sandalio LM, Palma JM, Bueno P, Corpas FJ (Nov 1992). "Metabolism of oxygen radicals in peroxisomes
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10. Corpas FJ, Barroso JB, del Río LA (Apr 2001). "Peroxisomes as a source of reactive oxygen species and nitric oxide
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11. Corpas FJ, Barroso JB, Carreras A, Quirós M, León AM, Romero-Puertas MC, Esteban FJ, Valderrama R, Palma JM,
Sandalio LM, Gómez M, del Río LA (Sep 2004). "Cellular and subcellular localization of endogenous nitric oxide in
young and senescent pea plants" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC523336). Plant Physiology. 136 (1):
2722–33. doi:10.1104/pp.104.042812 (https://doi.org/10.1104%2Fpp.104.042812). PMC 523336 (https://www.ncbi.nl
m.nih.gov/pmc/articles/PMC523336). PMID 15347796 (https://www.ncbi.nlm.nih.gov/pubmed/15347796).
12. Bednarek P, Pislewska-Bednarek M, Svatos A, Schneider B, Doubsky J, Mansurova M, Humphry M, Consonni C,
Panstruga R, Sanchez-Vallet A, Molina A, Schulze-Lefert P (Jan 2009). "A glucosinolate metabolism pathway in living
plant cells mediates broad-spectrum antifungal defense". Science. 323 (5910): 101–6. doi:10.1126/science.1163732
(https://doi.org/10.1126%2Fscience.1163732). PMID 19095900 (https://www.ncbi.nlm.nih.gov/pubmed/19095900).
13. Hoepfner D, Schildknegt D, Braakman I, Philippsen P, Tabak HF (Jul 2005). "Contribution of the endoplasmic
reticulum to peroxisome formation" (http://dspace.library.uu.nl:8080/handle/1874/9833). Cell. 122 (1): 85–95.
doi:10.1016/j.cell.2005.04.025 (https://doi.org/10.1016%2Fj.cell.2005.04.025). PMID 16009135 (https://www.ncbi.nlm.
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14. Saleem RA, Smith JJ, Aitchison JD (Dec 2006). "Proteomics of the peroxisome" (https://www.ncbi.nlm.nih.gov/pmc/ar
ticles/PMC1858641). Biochimica et Biophysica Acta. 1763 (12): 1541–51. doi:10.1016/j.bbamcr.2006.09.005 (https://d
oi.org/10.1016%2Fj.bbamcr.2006.09.005). PMC 1858641 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1858641).
PMID 17050007 (https://www.ncbi.nlm.nih.gov/pubmed/17050007).
15. Dammai V, Subramani S (Apr 2001). "The human peroxisomal targeting signal receptor, Pex5p, is translocated into
the peroxisomal matrix and recycled to the cytosol". Cell. 105 (2): 187–96. doi:10.1016/s0092-8674(01)00310-5 (http
s://doi.org/10.1016%2Fs0092-8674%2801%2900310-5). PMID 11336669 (https://www.ncbi.nlm.nih.gov/pubmed/1133
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16. Depreter M, Espeel M, Roels F (Jun 2003). "Human peroxisomal disorders". Microscopy Research and Technique. 61
(2): 203–23. doi:10.1002/jemt.10330 (https://doi.org/10.1002%2Fjemt.10330). PMID 12740827 (https://www.ncbi.nlm.
nih.gov/pubmed/12740827).
17. Depreter M, Espeel M, Roels F (Jun 2003). "Human peroxisomal disorders" (http://www.springerlink.com/content/014
1-8955/18/s1/). Microscopy Research and Technique. 61 (2): 203–23. doi:10.1002/jemt.10330 (https://doi.org/10.100
2%2Fjemt.10330). PMID 12740827 (https://www.ncbi.nlm.nih.gov/pubmed/12740827).
18. Lazarow PB, Fujiki Y (1985). "Biogenesis of peroxisomes". Annual Review of Cell Biology. 1: 489–530.
doi:10.1146/annurev.cb.01.110185.002421 (https://doi.org/10.1146%2Fannurev.cb.01.110185.002421).
PMID 3916321 (https://www.ncbi.nlm.nih.gov/pubmed/3916321).
19. Fagarasanu A, Fagarasanu M, Rachubinski RA (2007). "Maintaining peroxisome populations: a story of division and
inheritance". Annual Review of Cell and Developmental Biology. 23: 321–44.
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20. Schlüter A, Fourcade S, Ripp R, Mandel JL, Poch O, Pujol A (Apr 2006). "The evolutionary origin of peroxisomes: an
ER-peroxisome connection". Molecular Biology and Evolution. 23 (4): 838–45. doi:10.1093/molbev/msj103 (https://do
i.org/10.1093%2Fmolbev%2Fmsj103). PMID 16452116 (https://www.ncbi.nlm.nih.gov/pubmed/16452116).
21. Gabaldón T, Snel B, van Zimmeren F, Hemrika W, Tabak H, Huynen MA (2006). "Origin and evolution of the
peroxisomal proteome" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1472686). Biology Direct. 1: 8.
doi:10.1186/1745-6150-1-8 (https://doi.org/10.1186%2F1745-6150-1-8). PMC 1472686 (https://www.ncbi.nlm.nih.gov/
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22. Duhita N, Le HA, Satoshi S, Kazuo H, Daisuke M, Takao S (Jan 2010). "The origin of peroxisomes: The possibility of
an actinobacterial symbiosis". Gene. 450 (1–2): 18–24. doi:10.1016/j.gene.2009.09.014 (https://doi.org/10.1016%2Fj.
gene.2009.09.014). PMID 19818387 (https://www.ncbi.nlm.nih.gov/pubmed/19818387).
23. Gabaldón T, Capella-Gutiérrez S (Oct 2010). "Lack of phylogenetic support for a supposed actinobacterial origin of
peroxisomes". Gene. 465 (1–2): 61–5. doi:10.1016/j.gene.2010.06.004 (https://doi.org/10.1016%2Fj.gene.2010.06.00
4). PMID 20600706 (https://www.ncbi.nlm.nih.gov/pubmed/20600706).
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ncbi.nlm.nih.gov/pmc/articles/PMC2289717). The Journal of Cell Biology. 119 (5): 1129–36.
doi:10.1083/jcb.119.5.1129 (https://doi.org/10.1083%2Fjcb.119.5.1129). PMC 2289717 (https://www.ncbi.nlm.nih.gov/
pmc/articles/PMC2289717). PMID 1447292 (https://www.ncbi.nlm.nih.gov/pubmed/1447292).

Further reading
Mateos RM, León AM, Sandalio LM, Gómez M, del Río LA, Palma JM (Dec 2003). "Peroxisomes from pepper fruits
(Capsicum annuum L.): purification, characterisation and antioxidant activity". Journal of Plant Physiology. 160 (12):
1507–16. doi:10.1078/0176-1617-01008 (https://doi.org/10.1078%2F0176-1617-01008). PMID 14717445 (https://ww
w.ncbi.nlm.nih.gov/pubmed/14717445).
Corpas FJ, Barroso JB (2014). "Functional implications of peroxisomal nitric oxide (NO) in plants" (https://www.ncbi.nl
m.nih.gov/pmc/articles/PMC3956114). Frontiers in Plant Science. 5: 97. doi:10.3389/fpls.2014.00097 (https://doi.org/1
0.3389%2Ffpls.2014.00097). PMC 3956114 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3956114).
PMID 24672535 (https://www.ncbi.nlm.nih.gov/pubmed/24672535).

Corpas FJ (2015). "What is the role of hydrogen peroxide in plant peroxisomes?". Plant Biol (Stuttg). 17 (6): 1099–
103. doi:10.1111/plb.12376 (https://doi.org/10.1111%2Fplb.12376). PMID 26242708 (https://www.ncbi.nlm.nih.gov/pub
med/26242708).

External links
PeroxisomeDB: Peroxisome-Database (http://www.peroxisomeDB.org)
PeroxisomeKB: Peroxisome Knowledge Base (http://www.peroxisomekb.nl)

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This article incorporates public domain material from the NCBI document "Science Primer" (https://www.ncbi.nlm.ni
h.gov/About/primer/index.html).

This article incorporates text from the public domain Pfam and InterPro: IPR006708 (https://ww
w.ebi.ac.uk/interpro/entry/IPR006708)

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