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ERT has also been used to treat patients with severe combined immunodeficiency (SCID) resulting from an adenosine deaminase deficiency . [2] Other treatment options for patients with enzyme or protein deficiencies include substrate reduction therapy, gene therapy, and bone-marrow derived stem cell transplantation. [1] [3] [4]
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7 ...
Catalase-peroxidase (EC 1.11.1.21, katG ... This enzyme is a strong catalase with H 2 O 2 as donor which releases O 2. References External links ...
Peroxidase can be used for treatment of industrial waste waters. For example, phenols, which are important pollutants, can be removed by enzyme-catalyzed polymerization using horseradish peroxidase. Thus phenols are oxidized to phenoxy radicals, which participate in reactions where polymers and oligomers are produced that are less toxic than ...
Acatalasia is an autosomal recessive peroxisomal disorder caused by absent or very low levels of the enzyme catalase. [2] Catalase breaks down hydrogen peroxide in cells into water and oxygen. Low levels of catalase can cause hydrogen peroxide to build up, causing damage to cells.
D-Bifunctional protein deficiency is an autosomal recessive peroxisomal fatty acid oxidation disorder. Peroxisomal disorders are usually caused by a combination of peroxisomal assembly defects or by deficiencies of specific peroxisomal enzymes. The peroxisome is an organelle in the cell similar to the lysosome that functions to detoxify the cell.
NAA also affects multiple antioxidant enzymes, such as catalase and glutathione peroxidase, impairing the detoxification of hydrogen peroxide. [24] Recent animal studies have shown the chronic oxidative stress may cause dysfunction in mitochondria, rendering the brain more susceptible to epileptic seizures. [24] [25]
The cytosols of virtually all eukaryotic cells contain a SOD enzyme with copper and zinc (Cu-Zn-SOD). For example, Cu-Zn-SOD available commercially is normally purified from bovine red blood cells. The bovine Cu-Zn enzyme is a homodimer of molecular weight 32,500. It was the first SOD whose atomic-detail crystal structure was solved, in 1975. [10]