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  2. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen. [5]

  3. Microbody - Wikipedia

    en.wikipedia.org/wiki/Microbody

    It contains enzymes like oxidase, react hydrogen peroxide as a byproduct of its enzymatic reactions. Within the peroxisome, hydrogen peroxide can then be converted to water by enzymes like catalase and peroxidase. Discovered and named by Christian de Duve.

  4. Peroxisome - Wikipedia

    en.wikipedia.org/wiki/Peroxisome

    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 (H 2 O 2, itself toxic):

  5. Obligate anaerobe - Wikipedia

    en.wikipedia.org/wiki/Obligate_anaerobe

    Aerobic organisms produce superoxide dismutase and catalase to detoxify these products, but obligate anaerobes produce these enzymes in very small quantities, or not at all. [1] [2] [3] [5] The variability in oxygen tolerance of obligate anaerobes (<0.5 to 8% O 2) is thought to reflect the quantity of superoxide dismutase and catalase being ...

  6. Haem peroxidase - Wikipedia

    en.wikipedia.org/wiki/Haem_peroxidase

    Class I, the intracellular peroxidases, includes: cytochrome c peroxidase (CCP), a soluble protein found in the mitochondrial electron transport chain, where it probably protects against toxic peroxides; ascorbate peroxidase (AP), the main enzyme responsible for hydrogen peroxide removal in chloroplasts and cytosol of higher plants; [4] and ...

  7. Peroxidase - Wikipedia

    en.wikipedia.org/wiki/Peroxidase

    For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues. The nature of the electron donor is very dependent on the structure ...

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  9. Beta oxidation - Wikipedia

    en.wikipedia.org/wiki/Beta_oxidation

    The enzyme catalase, found primarily in peroxisomes and the cytosol of erythrocytes (and sometimes in mitochondria [12]), converts the hydrogen peroxide into water and oxygen. Peroxisomal β-oxidation also requires enzymes specific to the peroxisome and to very long fatty acids.

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