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  2. Phosphatase - Wikipedia

    en.wikipedia.org/wiki/Phosphatase

    Water is split in the reaction, with the -OH group attaching to the phosphate ion, and the H+ protonating the hydroxyl group of the other product. The net result of the reaction is the destruction of a phosphomonoester and the creation of both a phosphate ion and a molecule with a free hydroxyl group. [4]

  3. 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]

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many therapeutic drugs and poisons are enzyme inhibitors.

  5. Carbonic anhydrase - Wikipedia

    en.wikipedia.org/wiki/Carbonic_anhydrase

    An enzyme is a substance that acts as a catalyst in living organisms which helps to speed up chemical reactions. [12] Carbonic anhydrase is one important enzyme that is found in red blood cells, gastric mucosa, pancreatic cells, and even renal tubules. It was discovered in the year 1932 and it has been categorized into three general classes. [13]

  6. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). [1] The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. [1]

  7. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    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 7.5. [9] The pH optimum for other catalases varies between 4 and 11 depending on the ...

  8. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    However, since enzymes are large molecules, they can position both acid groups and basic groups in their active site to interact with their substrates, and employ both modes independent of the bulk pH. [citation needed] Often general acid or base catalysis is employed to activate nucleophile and/or electrophile groups, or to stabilize leaving ...

  9. Dephosphorylation - Wikipedia

    en.wikipedia.org/wiki/Dephosphorylation

    Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate. Dephosphorylation employs a type of hydrolytic enzyme, or hydrolase, which cleaves