Peroxisome

A peroxisome () is a membrane-bound organelle, a type of microbody, found in the cytoplasm of virtually all eukaryotic cells. Peroxisomes are oxidative organelles. Frequently, molecular oxygen serves as a co-substrate, from which hydrogen peroxide (H2O2) is then formed. Peroxisomes owe their name to hydrogen peroxide-generating and scavenging activities. They perform key roles in lipid metabolism and the reduction of reactive oxygen species. Peroxisomes are involved in the catabolism of very long chain fatty acids, branched chain fatty acids, bile acid intermediates (in the liver), D-amino acids, and polyamines. Peroxisomes also play a role in the biosynthesis of plasmalogens: ether phospholipids critical for the normal function of mammalian brains and lungs. Peroxisomes contain approximately 10% of the total activity of two enzymes (Glucose-6-phosphate dehydrogenase and 6-Phosphogluconate dehydrogenase) in the pentose phosphate pathway, which is important for energy metabolism. It is debated whether peroxisomes are involved in isoprenoid and cholesterol synthesis in animals. Other peroxisomal functions include the glyoxylate cycle in germinating seeds ("glyoxysomes"), photorespiration in leaves, glycolysis in trypanosomes ("glycosomes"), and methanol and amine oxidation and assimilation in some yeasts.

History Peroxisomes (microbodies) were first described by a Swedish doctoral student, J. Rhodin in 1954. They were identified as organelles by Christian de Duve and Pierre Baudhuin in 1966. De Duve and co-workers discovered that peroxisomes contain several oxidases involved in the production of hydrogen peroxide (H2O2) as well as catalase involved in the decomposition of H2O2 to oxygen and water. Due to their role in peroxide metabolism, De Duve named them "peroxisomes", replacing the formerly used morphological term "microbodies". Later, it was described that firefly luciferase is targeted to peroxisomes in mammalian cells, allowing the discovery of the import targeting signal for peroxisomes, and triggering many advances in the peroxisome biogenesis field.

Structure Peroxisomes are small (0.1–1 μm diameter) organelles with a fine, granular matrix, surrounded by a single biomembrane located in the cytoplasm of a cell. Compartmentalization creates an optimized environment to promote various metabolic reactions within peroxisomes required to sustain cellular functions and viability of the organism. The number, size, and protein composition of peroxisomes are variable and depend on cell type and environmental conditions. For example, in baker's yeast (S. cerevisiae), it has been observed that, with a good glucose supply, only a few, small peroxisomes are present. In contrast, when the yeasts were supplied with long-chain fatty acids as sole carbon source up to 20 to 25 large peroxisomes can be formed.

Metabolic functions 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 eventually are broken down to carbon dioxide and water. In yeast and plant cells, this process is carried out exclusively in peroxisomes. 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 nervous system. Peroxisomes also play a role in the production of bile acids 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. The specific metabolic pathways that occur exclusively in mammalian peroxisomes are:

α-oxidation of phytanic acid β-oxidation of very-long-chain and polyunsaturated fatty acids biosynthesis of plasmalogens conjugation of cholic acid as part of bile acid synthesis Peroxisomes contain oxidative enzymes, such as D-amino acid oxidase and uric acid oxidase. 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):

R H 2 + O 2 → R + H 2 O 2 {\displaystyle \mathrm {RH} _{\mathrm {2} }+\mathrm {O} _{\mathrm {2} }\rightarrow \mathrm {R} +\mathrm {H} _{2}\mathrm {O} _{2}}

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

H 2 O 2 + R ′ H 2 → R ′ + 2 H 2 O {\displaystyle \mathrm {H} _{2}\mathrm {O} _{2}+\mathrm {R'H} _{2}\rightarrow \mathrm {R'} +2\mathrm {H} _{2}\mathrm {O} } , 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 that humans consume by drinking alcoholic beverages is oxidized to acetaldehyde in this way. In addition, when excess H2O2 accumulates in the cell, catalase converts it to H2O through this reaction:

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