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  2. Peroxiredoxin - Wikipedia

    en.wikipedia.org/wiki/Peroxiredoxin

    Using high resolution crystal structures, a detailed catalytic cycle has been derived for Prxs, [8] including a model for the redox-regulated oligomeric state proposed to control enzyme activity. [9] These enzymes are inactivated by over-oxidation (also known as hyperoxidation ) of the active thiol to the sulfinic acid (RSO 2 H).

  3. Coenzyme A - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_A

    Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate.

  4. Antioxidant - Wikipedia

    en.wikipedia.org/wiki/Antioxidant

    The relative importance of the antioxidant and pro-oxidant activities of antioxidants is an area of current research, but vitamin C, which exerts its effects as a vitamin by oxidizing polypeptides, appears to have a mostly antioxidant action in the human body. [95]

  5. 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]

  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. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    The enzyme then changes shape again and forces these molecules together, with the active site in the resulting "tight" state (shown in pink) binding the newly produced ATP molecule with very high affinity. Finally, the active site cycles back to the open state, releasing ATP and binding more ADP and phosphate, ready for the next cycle.

  8. Heme oxygenase - Wikipedia

    en.wikipedia.org/wiki/Heme_oxygenase

    The human genome may encode three isoforms of HMOX. The degradation of heme forms three distinct chromogens as seen in healing cycle of a bruise. This reaction can occur in virtually every cell and platelet; the classic example is the healing process of a contusion , which forms different chromogens as it gradually heals: (red) heme to (green ...

  9. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...