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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. Fungal extracellular enzyme activity - Wikipedia

    en.wikipedia.org/wiki/Fungal_extracellular...

    Benefits of exoenzyme production can also be lost after secretion because the enzymes are liable to denature, degrade or diffuse away from the producer cell. Enzyme production and secretion is an energy intensive process [14] and, because it consumes resources otherwise available for reproduction, there is evolutionary pressure to conserve ...

  4. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    Polyphenol oxidase is an enzyme found throughout the plant and animal kingdoms, [31] including most fruits and vegetables. [32] PPO has importance to the food industry because it catalyzes enzymatic browning when tissue is damaged from bruising, compression or indentations, making the produce less marketable and causing economic loss.

  5. 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 ...

  6. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are asymmetrical molecules. For all standard amino acids, except glycine, the α-carbon is a chiral center. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this ...

  7. Ribonucleotide reductase - Wikipedia

    en.wikipedia.org/wiki/Ribonucleotide_reductase

    Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. [1] [2] It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates (or triphosphates depending on the class of RNR).

  8. Pectinase - Wikipedia

    en.wikipedia.org/wiki/Pectinase

    Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%), [4] but cannot be synthesized by animal or human cells. [5] In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made.

  9. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    [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. [2] Different metabolic pathways function in the position within a eukaryotic cell and the significance of the pathway in the given compartment of the cell. [3]