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  2. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second. [ 6 ] Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [ 7 ]

  3. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

  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. Nitrification - Wikipedia

    en.wikipedia.org/wiki/Nitrification

    Nitrification is important in agricultural systems, where fertilizer is often applied as ammonia. Conversion of this ammonia to nitrate increases nitrogen leaching because nitrate is more water-soluble than ammonia. Nitrification also plays an important role in the removal of nitrogen from municipal wastewater.

  7. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    That is, the chemical catalysis is defined as the reduction of E a ‡ (when the system is already in the ES ‡) relative to E a ‡ in the uncatalyzed reaction in water (without the enzyme). The induced fit only suggests that the barrier is lower in the closed form of the enzyme but does not tell us what the reason for the barrier reduction is.

  8. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.

  9. Ethanol fermentation - Wikipedia

    en.wikipedia.org/wiki/Ethanol_fermentation

    Fermentation does not require oxygen. If oxygen is present, some species of yeast (e.g., Kluyveromyces lactis or Kluyveromyces lipolytica) will oxidize pyruvate completely to carbon dioxide and water in a process called cellular respiration, hence these species of yeast will produce ethanol only in an anaerobic environment (not cellular ...