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  2. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    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 ...

  3. Superoxide dismutase - Wikipedia

    en.wikipedia.org/wiki/Superoxide_dismutase

    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]

  4. Pyrroloquinoline quinone - Wikipedia

    en.wikipedia.org/wiki/Pyrroloquinoline_quinone

    Efforts to understand PQQ biosynthesis have contributed to broad interest in radical SAM enzymes and their ability to modify proteins, and an analogous radical SAM enzyme-dependent pathway has since been found that produces the putative electron carrier mycofactocin, using a valine and a tyrosine from the precursor peptide, MftA

  5. Antioxidant - Wikipedia

    en.wikipedia.org/wiki/Antioxidant

    Catalases are enzymes that catalyse the conversion of hydrogen peroxide to water and oxygen, using either an iron or manganese cofactor. [103] [104] This protein is localized to peroxisomes in most eukaryotic cells. [105] Catalase is an unusual enzyme since, although hydrogen peroxide is its only substrate, it follows a ping-pong mechanism.

  6. Coenzyme Q10 - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_Q10

    Coenzyme Q 10 (CoQ 10 / ˌ k oʊ k j uː ˈ t ɛ n /), also known as ubiquinone, is a naturally occurring biochemical cofactor (coenzyme) and an antioxidant produced by the human body. [1] [2] [3] It can also be obtained from dietary sources, such as meat, fish, seed oils, vegetables, and dietary supplements.

  7. Catalase-peroxidase - Wikipedia

    en.wikipedia.org/wiki/Catalase-peroxidase

    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 ...

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  9. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]

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