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Peroxisomes (also called microbodies) are organelles found in virtually all eukaryotic cells. They are involved in the catabolism of very long chain fatty acids, branched chain fatty acids, D-amino acids, and polyamines, reduction of reactive oxygen species - specifically hydrogen peroxide - and biosynthesis of plasmalogens, i.e. ether phospholipids critical for the normal function of mammalian brains and lungs. They also contain approximately 10% of the total activity of two enzymes in the pentose phosphate pathway, which is important for energy metabolism.〔 It is vigorously debated if peroxisomes are involved in isoprenoid and cholesterol synthesis in animals.〔 Other known peroxisomal functions include the glyoxylate cycle in germinating seeds ("glyoxysomes"), photorespiration in leaves, glycolysis in trypanosomes ("glycosomes"), and methanol and/or amine oxidation and assimilation in some yeasts. Peroxisomes were identified as organelles by the Belgian cytologist Christian de Duve in 1967 after they had been first described by a Swedish doctoral student, J. Rhodin in 1954. == 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 are eventually broken down to carbon dioxide and water. In yeast and plant cells, this process is exclusive for the 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. Peroxisomes contain oxidative enzymes, such as catalase, 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): : 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.〔 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. 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). 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Peroxisome」の詳細全文を読む スポンサード リンク
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