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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Superoxide dismutase - Wikipedia

    en.wikipedia.org/wiki/Superoxide_dismutase

    Superoxide is known to denature enzymes, oxidize lipids, and fragment DNA. [21] SODs catalyze the production of O 2 and H 2 O 2 from superoxide (O − 2), which results in less harmful reactants. When acclimating to increased levels of oxidative stress, SOD concentrations typically increase with the degree of stress conditions.

  4. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. [1]

  5. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  7. RuBisCO - Wikipedia

    en.wikipedia.org/wiki/RuBisCo

    RuBisCO is important biologically because it catalyzes the primary chemical reaction by which inorganic carbon enters the biosphere.While many autotrophic bacteria and archaea fix carbon via the reductive acetyl CoA pathway, the 3-hydroxypropionate cycle, or the reverse Krebs cycle, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO.

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.

  9. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes. [1]: 26 In most cases of a metabolic pathway, the product of one enzyme acts as the substrate for the next. However, side products are considered waste and removed from the cell.